ACOX1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005504 fatty acid binding	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Retain inherited fatty-acid binding with a bounded structural interpretation. Reason: GO:0005504 describes binding to a fatty acid and does not require a dedicated carrier site. Rat ACOX1 structure 2DDH (P07872; PMID:16672280) contains free hydroxydodecanoic acid in the active-site channel after hydrolysis of the crystallization acyl-CoA ligand. The free carboxyl group makes defined hydrogen-bond contacts with the enzyme/FAD environment; this observed noncovalent complex supports fatty-acid binding even though the ligand arose in the crystal and occupies the substrate channel. Retain this ortholog-supported capability as non-core, with no claim of a separate binding site, physiological carrier function, or measured free-acid affinity in human ACOX1. The PAINT IBD is on PTN000097533; exact free-acid-binding assays for its Acox2/Acox3 donors remain unresolved. Retention is supported independently by the ACOX1 ortholog structure, not by assuming those donor assays measured free acid. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000097533 UNRESOLVED The cached PAINT IBD (2025-09-02) is seeded by rat Acox2/Acox3 fatty-acid-binding evidence. Exact donor assay details remain unresolved; no target-specific loss is established. Independent rat ACOX1 ligand-bound structure supports retention of a non-core inherited capability. Supporting Evidence: PMID:16672280 only the fatty acid moiety that had been formed through hydrolysis of the thioester bond
GO:0033540 fatty acid beta-oxidation using acyl-CoA oxidase	IBA GO_REF:0000033	ACCEPT	Summary: ACOX1 catalyzes the oxidase step of peroxisomal fatty-acid beta-oxidation. Reason: The PAINT inference agrees with direct human oxidase chemistry, rather than merely inferring a process from disease association. ACOX1 performs the initial reaction itself. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097533 SUPPORTS TRANSFER Cached PAINT IBD (2026-08-28) uses human Q15067 experimental evidence at this ancestral node. Target self-evidence is legitimate grounding for inheritance; human catalytic chemistry agrees. Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0120524 long-chain fatty acyl-CoA oxidase activity	IBA GO_REF:0000033	ACCEPT	Summary: Long-chain acyl-CoA oxidase activity is directly supported for human ACOX1. Reason: Purified recombinant human enzyme has maximal activity with C12–18 saturated substrates and measured palmitoyl-CoA kinetics. These data support the inherited long-chain activity independently of the isoform summary. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097706 SUPPORTS TRANSFER Cached PAINT IBD (2025-09-02) places long-chain oxidase activity at this chordate node, including human Q15067 evidence. Human palmitoyl-CoA assays independently corroborate retained activity. Supporting Evidence: PMID:7876265 Using the purified enzyme, Km and Vmax values for palmitoyl-CoA were found to be 10 microM and 1.4 units/mg of protein, respectively. PMID:7876265 The maximal activities for saturated fatty acids were observed with C12-18 substrates.
GO:0005777 peroxisome	IBA GO_REF:0000033	ACCEPT	Summary: Peroxisomes are the established functional compartment. Reason: The ancestral placement is consistent with human ACOX1 PTS1 targeting and direct colocalization of expressed wild-type human ACOX1 with eYFP-PTS1 in the fly model. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097533 SUPPORTS TRANSFER Cached PAINT IBD (2025-04-11) includes human Q15067 experimental evidence. Human PTS1 and localization data agree with inheritance; no target-specific localization loss is apparent. Supporting Evidence: PMID:32169171 both hACOX1WT and hACOX1N237S are localized to peroxisomes PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal
GO:0050660 flavin adenine dinucleotide binding	IBA GO_REF:0000033	ACCEPT	Summary: FAD is the oxidase redox cofactor. Reason: The inherited cofactor-binding annotation agrees with the human UniProt cofactor record and the FAD-containing rat ACOX1 structural assembly. FAD binding is a component of the oxidase function, not a separate biological role. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097533 SUPPORTS TRANSFER Cached PAINT IBD (2024-11-19) includes human Q15067 grounding for FAD binding. The conserved flavoprotein mechanism and cofactor record agree. Supporting Evidence: file:human/ACOX1/ACOX1-uniprot.txt Name=FAD; Xref=ChEBI:CHEBI:57692;
GO:0000038 very long-chain fatty acid metabolic process	IBA GO_REF:0000033	ACCEPT	Summary: ACOX1 directly participates in very-long-chain fatty-acid metabolism. Reason: Patient fibroblast enzyme deficiency and abnormal plasma VLCFAs support the human pathway; the oxidase chemistry establishes catalytic participation. The target human evidence underlying the PAINT node is legitimate experimental grounding. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097706 SUPPORTS TRANSFER Cached PAINT IBD (2021-05-29) includes human Q15067 experimental grounding for VLCFA metabolism. Patient enzyme deficiency and the oxidase reaction support retention. Supporting Evidence: PMID:18536048 Studies in fibroblasts from the two patients revealed a deficiency of one of the two peroxisomal acyl-CoA oxidases, that is, straight-chain acyl-CoA oxidase (ACOX1). PMID:18536048 Plasma very-long-chain fatty acids were abnormal in both patients PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0003997 acyl-CoA oxidase activity	IEA GO_REF:0000120	ACCEPT	Summary: Acyl-CoA oxidase is the experimentally established molecular function. Reason: The combined EC, domain, orthology and Rhea mapping agrees with purified human palmitoyl-CoA oxidation. Oxygen receives the reducing equivalents and H2O2 is produced; an ETF-dependent acyl-CoA dehydrogenase term would describe different electron-transfer chemistry. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P07872 SUPPORTS TRANSFER Rat ACOX1 is the experimentally studied ortholog in PDB2DDH, with FAD and C2 homodimer organization. Human ACOX1 assays independently support the relevant catalytic, cofactor, localization or self-association assertion; paralogous ACOX2 is not this donor. ENSEMBL:ENSRNOP00000051538 UNRESOLVED The GOA-listed rat donor protein record and its exact experimental source chain were not retrieved. Independent human ACOX1 evidence supports the reviewed function/location, without inventing donor assay details. InterPro:IPR002655 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. InterPro:IPR012258 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. InterPro:IPR034171 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. RHEA:38959 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:40275 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:40315 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. EC:1.3.3.6 SUPPORTS TRANSFER EC1.3.3.6 denotes acyl-CoA oxidase chemistry, with oxygen as acceptor, matching recombinant human ACOX1 enzymology. Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2. PMID:7876265 Using the purified enzyme, Km and Vmax values for palmitoyl-CoA were found to be 10 microM and 1.4 units/mg of protein, respectively.
GO:0005504 fatty acid binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: Retain the family-mapped fatty-acid recognition capability as non-core. Reason: GO:0005504 describes binding to a fatty acid and does not require a dedicated carrier site. Rat ACOX1 structure 2DDH (P07872; PMID:16672280) contains free hydroxydodecanoic acid in the active-site channel after hydrolysis of the crystallization acyl-CoA ligand. The free carboxyl group makes defined hydrogen-bond contacts with the enzyme/FAD environment; this observed noncovalent complex supports fatty-acid binding even though the ligand arose in the crystal and occupies the substrate channel. Retain this ortholog-supported capability as non-core, with no claim of a separate binding site, physiological carrier function, or measured free-acid affinity in human ACOX1. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: InterPro:IPR034171 SUPPORTS TRANSFER The ACOX1 family mapping is compatible with the free ligand observed in the rat ACOX1 crystal structure. Retain recognition as non-core without inferring a carrier role. Supporting Evidence: PMID:16672280 only the fatty acid moiety that had been formed through hydrolysis of the thioester bond
GO:0005777 peroxisome	IEA GO_REF:0000120	ACCEPT	Summary: The combined electronic peroxisome assignment is experimentally corroborated. Reason: Human ACOX1 contains the SKL targeting signal and colocalizes with a peroxisomal marker. The independent experimental support is more decisive than treating family membership alone as proof of localization. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P07872 SUPPORTS TRANSFER Rat ACOX1 is the experimentally studied ortholog in PDB2DDH, with FAD and C2 homodimer organization. Human ACOX1 assays independently support the relevant catalytic, cofactor, localization or self-association assertion; paralogous ACOX2 is not this donor. ENSEMBL:ENSRNOP00000051538 UNRESOLVED The GOA-listed rat donor protein record and its exact experimental source chain were not retrieved. Independent human ACOX1 evidence supports the reviewed function/location, without inventing donor assay details. InterPro:IPR002655 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. InterPro:IPR012258 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. UniProtKB-SubCell:SL-0204 SUPPORTS TRANSFER The UniProt subcellular-location mapping is consistent with human PTS1 targeting and independent peroxisomal colocalization; it is a location vocabulary mapping, not another experiment. Supporting Evidence: PMID:32169171 both hACOX1WT and hACOX1N237S are localized to peroxisomes PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal
GO:0005782 peroxisomal matrix	IEA GO_REF:0000117	ACCEPT	Summary: ACOX1 acts in the peroxisomal matrix. Reason: The PTS1-containing enzyme is imported as peroxisomal cargo. Reactome describes release of cargo into the matrix, consistent with ACOX1 biochemical function; the exact ARBA rule internals were not recovered. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00088448 UNRESOLVED Exact rule conditions and training assertions were not recovered. The annotation judgment instead follows independent human enzyme/targeting evidence; it does not claim an audit of unseen model internals. Supporting Evidence: PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal Reactome:R-HSA-9033235 the cargo protein is released into the peroxisomal matrix
GO:0006631 fatty acid metabolic process	IEA GO_REF:0000002	MODIFY	Summary: Refine broad fatty-acid metabolism to fatty-acid beta-oxidation. Reason: The InterPro inference is biologically correct but broader than the directly established oxidative step. This is a specificity refinement, not evidence that fatty-acid metabolism is false. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR012258 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. Proposed replacements: fatty acid beta-oxidation Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0006635 fatty acid beta-oxidation	IEA GO_REF:0000002	ACCEPT	Summary: ACOX1 performs the initial oxidative reaction in fatty-acid beta-oxidation. Reason: The InterPro mapping is corroborated by human enzymology and the peroxisomal pathway. This is direct catalytic participation, not a secondary response to lipid accumulation. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR002655 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2. PMID:18536048 Studies in fibroblasts from the two patients revealed a deficiency of one of the two peroxisomal acyl-CoA oxidases, that is, straight-chain acyl-CoA oxidase (ACOX1).
GO:0016491 oxidoreductase activity	IEA GO_REF:0000117	MODIFY	Summary: Refine oxidoreductase activity to acyl-CoA oxidase activity. Reason: The broad ARBA assignment is chemically correct. Human enzyme studies establish the donor substrate class and direct oxygen reduction, permitting a specific oxidase term without inventing a new function. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: ARBA:ARBA00028747 UNRESOLVED Exact rule conditions and training assertions were not recovered. The annotation judgment instead follows independent human enzyme/targeting evidence; it does not claim an audit of unseen model internals. Proposed replacements: acyl-CoA oxidase activity Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors	IEA GO_REF:0000002	MODIFY	Summary: Refine the CH-CH oxidoreductase class to acyl-CoA oxidase activity. Reason: The domain mapping captures the correct reaction class but omits the acyl-CoA substrate and oxygen acceptor. Direct human enzymology supports the replacement. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR006091 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. InterPro:IPR009100 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. InterPro:IPR036250 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. InterPro:IPR037069 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. InterPro:IPR046373 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. Proposed replacements: acyl-CoA oxidase activity Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0033540 fatty acid beta-oxidation using acyl-CoA oxidase	IEA GO_REF:0000120	ACCEPT	Summary: The combined mapping identifies the actual peroxisomal oxidase pathway. Reason: The pathway, domain and ortholog sources converge on a function independently established by the human oxidase assay. The particular ARBA model internals remain unresolved; acceptance does not depend on reconstructing those internals. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00085031 UNRESOLVED Exact rule conditions and training assertions were not recovered. The annotation judgment instead follows independent human enzyme/targeting evidence; it does not claim an audit of unseen model internals. UniProtKB:P07872 SUPPORTS TRANSFER Rat ACOX1 is the experimentally studied ortholog in PDB2DDH, with FAD and C2 homodimer organization. Human ACOX1 assays independently support the relevant catalytic, cofactor, localization or self-association assertion; paralogous ACOX2 is not this donor. ENSEMBL:ENSRNOP00000051538 UNRESOLVED The GOA-listed rat donor protein record and its exact experimental source chain were not retrieved. Independent human ACOX1 evidence supports the reviewed function/location, without inventing donor assay details. InterPro:IPR034171 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. UniPathway:UPA00661 SUPPORTS TRANSFER The UniProt pathway cross-reference places ACOX1 in peroxisomal fatty-acid beta-oxidation, consistent with its demonstrated oxidative reaction. Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0044535 very-long-chain fatty acyl-CoA oxidase activity	IEA GO_REF:0000116	ACCEPT	Summary: Retain the curated very-long-chain acyl-CoA oxidase activity. Reason: The Rhea reaction set in UniProt includes very-long-chain acyl-CoA oxidation, consistent with human ACOX1-deficient fibroblasts and VLCFA accumulation. These curated substrate mappings should not all be represented as individually measured purified-human reactions; nevertheless the very-long-chain activity class is well supported. Propagation Review Root cause: NO FAILURE CORE Sources checked: RHEA:39119 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:39135 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:40319 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:78631 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:78847 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:83047 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. Supporting Evidence: file:human/ACOX1/ACOX1-uniprot.txt shows activity towards long-chain and very-long-chain PMID:18536048 Studies in fibroblasts from the two patients revealed a deficiency of one of the two peroxisomal acyl-CoA oxidases, that is, straight-chain acyl-CoA oxidase (ACOX1). PMID:18536048 Plasma very-long-chain fatty acids were abnormal in both patients
GO:0050660 flavin adenine dinucleotide binding	IEA GO_REF:0000120	ACCEPT	Summary: FAD binding is an established property of ACOX1. Reason: The combined orthology/domain inference agrees with the curated human cofactor assignment and retained oxidase chemistry. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P07872 SUPPORTS TRANSFER Rat ACOX1 is the experimentally studied ortholog in PDB2DDH, with FAD and C2 homodimer organization. Human ACOX1 assays independently support the relevant catalytic, cofactor, localization or self-association assertion; paralogous ACOX2 is not this donor. ENSEMBL:ENSRNOP00000051538 UNRESOLVED The GOA-listed rat donor protein record and its exact experimental source chain were not retrieved. Independent human ACOX1 evidence supports the reviewed function/location, without inventing donor assay details. InterPro:IPR037069 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. Supporting Evidence: file:human/ACOX1/ACOX1-uniprot.txt Name=FAD; Xref=ChEBI:CHEBI:57692;
GO:0071949 FAD binding	IEA GO_REF:0000002	ACCEPT	Summary: FAD binding supports the oxidase catalytic mechanism. Reason: The acyl-CoA oxidase family and ACOX1 family domains map to cofactor binding consistently with the human UniProt record. Retain this cofactor annotation within the integrated oxidase core. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR012258 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. InterPro:IPR034171 SUPPORTS TRANSFER This domain/family record occurs in the human UniProt cross-references. It supports the encoded enzyme class; the reviewed specificity and cellular role are checked against human biochemistry and targeting evidence rather than inferred from domain presence alone. Supporting Evidence: file:human/ACOX1/ACOX1-uniprot.txt Name=FAD; Xref=ChEBI:CHEBI:57692;
GO:0120523 medium-chain fatty acyl-CoA oxidase activity	IEA GO_REF:0000116	ACCEPT	Summary: Medium-chain acyl-CoA oxidase activity is part of the documented substrate range. Reason: Rhea mappings include decanoyl-, dodecanoyl- and other medium-chain reactions. Human recombinant enzyme is active with C12 substrates, and the curated isoform-1 record identifies a C10 optimum. The original isoform-comparison full papers were unavailable after normal fetch failure; no additional isoform-exclusive assay details are asserted. Propagation Review Root cause: NO FAILURE CORE Sources checked: RHEA:40171 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:40175 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:40179 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:40311 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:78855 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. Supporting Evidence: PMID:7876265 The maximal activities for saturated fatty acids were observed with C12-18 substrates. file:human/ACOX1/ACOX1-uniprot.txt Shows highest activity against medium-chain
GO:0042803 protein homodimerization activity	IEA GO_REF:0000107	ACCEPT	Summary: Homodimerization is supported independently of the orthology transfer. Reason: Human Flag- and V5-tagged ACOX1 co-immunoprecipitation in primary Schwann cells supports self-association (PMID:32169171, Figure 6E). The 2020 paper refers to earlier structural work; it did not itself solve a human crystal structure. The rat 2DDH biological assembly independently has C2 homodimer organization. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P07872 SUPPORTS TRANSFER Rat ACOX1 is the experimentally studied ortholog in PDB2DDH, with FAD and C2 homodimer organization. Human ACOX1 assays independently support the relevant catalytic, cofactor, localization or self-association assertion; paralogous ACOX2 is not this donor. ENSEMBL:ENSRNOP00000051538 UNRESOLVED The GOA-listed rat donor protein record and its exact experimental source chain were not retrieved. Independent human ACOX1 evidence supports the reviewed function/location, without inventing donor assay details. Supporting Evidence: PMID:32169171 We transfected 4 different combinations of ACOX1 constructs with different tags into primary Schwann cells 1) Flag-ACOX1WT + V5-ACOX1WT
GO:0120524 long-chain fatty acyl-CoA oxidase activity	IEA GO_REF:0000120	ACCEPT	Summary: Retain the combined long-chain oxidase inference. Reason: The Rhea mappings and rat orthology agree with direct palmitoyl-CoA kinetics and C12–18 maximal activity of recombinant human ACOX1. This acceptance does not require claiming every listed Rhea substrate was individually assayed in that paper. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P07872 SUPPORTS TRANSFER Rat ACOX1 is the experimentally studied ortholog in PDB2DDH, with FAD and C2 homodimer organization. Human ACOX1 assays independently support the relevant catalytic, cofactor, localization or self-association assertion; paralogous ACOX2 is not this donor. ENSEMBL:ENSRNOP00000051538 UNRESOLVED The GOA-listed rat donor protein record and its exact experimental source chain were not retrieved. Independent human ACOX1 evidence supports the reviewed function/location, without inventing donor assay details. RHEA:38971 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:40167 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:40183 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:69643 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:78571 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:78587 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:78851 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. RHEA:83059 SUPPORTS TRANSFER This reaction identifier occurs in the human UniProt catalytic-activity record. Its oxygen-dependent acyl-CoA-to-enoyl-CoA chemistry and substrate class support the mapped oxidase activity; curated reaction attribution is not a claim that each substrate was assayed in a purified-human experiment. Supporting Evidence: PMID:7876265 Using the purified enzyme, Km and Vmax values for palmitoyl-CoA were found to be 10 microM and 1.4 units/mg of protein, respectively. PMID:7876265 The maximal activities for saturated fatty acids were observed with C12-18 substrates.
GO:0140493 very long-chain fatty acid beta-oxidation	IMP PMID:32169171 Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Lo...	ACCEPT	Summary: ACOX1 catalysis supports very-long-chain fatty-acid beta-oxidation. Reason: PMID:32169171 shows elevated VLCFA ratios after dACOX1 loss and studies human constructs; independent ACOX1-deficient patient fibroblasts support the human pathway. The gain-of-function fly model did not show the same VLCFA accumulation, so its toxicity should not be conflated with loss-of-function lipid blockade. Supporting Evidence: PMID:32169171 observed increased levels of total VLCFA, C28/C22, and C26/C22 in dACOX1T2A mutants PMID:18536048 Studies in fibroblasts from the two patients revealed a deficiency of one of the two peroxisomal acyl-CoA oxidases, that is, straight-chain acyl-CoA oxidase (ACOX1).
GO:0005777 peroxisome	IDA PMID:32169171 Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Lo...	ACCEPT	Summary: Expressed human ACOX1 colocalizes with a peroxisomal marker. Reason: Figure 4C in PMID:32169171 examines human wild-type and N237S proteins in fly salivary glands using eYFP-PTS1. Preserve the direct localization annotation with this experimental-system scope. Supporting Evidence: PMID:32169171 both hACOX1WT and hACOX1N237S are localized to peroxisomes
GO:0009062 fatty acid catabolic process	IMP PMID:32169171 Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Lo...	ACCEPT	Summary: ACOX1 participates catalytically in fatty-acid catabolism. Reason: The source establishes lipid accumulation after loss of dACOX1, while direct human oxidase chemistry explains the catalytic step in degradation. The broad catabolic term remains correct; no additional process annotation is necessary. Supporting Evidence: PMID:32169171 observed increased levels of total VLCFA, C28/C22, and C26/C22 in dACOX1T2A mutants PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0042803 protein homodimerization activity	IDA PMID:32169171 Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Lo...	ACCEPT	Summary: Human ACOX1 self-association is demonstrated by tagged-protein co-immunoprecipitation. Reason: Figure 6E compares wild-type/wild-type, mutant/mutant and mixed human ACOX1 pairs in primary Schwann cells. Methods identify the primary cultures as rat-derived. Mutant dimers are more abundant, but wild-type interaction is also tested. Anchor this IDA to those experiments rather than the introductory citation to prior crystal structures. Supporting Evidence: PMID:32169171 We transfected 4 different combinations of ACOX1 constructs with different tags into primary Schwann cells 1) Flag-ACOX1WT + V5-ACOX1WT
GO:0003997 acyl-CoA oxidase activity	IMP PMID:32169171 Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Lo...	ACCEPT	Summary: Wild-type and N237S ACOX1 are assayed for acyl-CoA oxidase activity. Reason: The protein-normalized assay reports about 40% greater activity for N237S than wild type. This directly tests the enzyme activity, independently of the clinical phenotype or introductory functional summary. Supporting Evidence: PMID:32169171 The data show that ACOX1N237S is more active by ~40% than ACOX1WT protein when normalized for protein levels
GO:0050665 hydrogen peroxide biosynthetic process	IMP PMID:32169171 Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Lo...	ACCEPT	Summary: Hydrogen peroxide is a direct product of the ACOX1 oxidase reaction. Reason: PMID:32169171 measures H2O2 in the overexpression model and studies antioxidant/catalase rescue. The enzymatic oxygen-to-H2O2 reaction is independently stated in the human enzyme characterization. Catalase consumes H2O2; that consumption alone would not establish ACOX1 production. Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2. PMID:32169171 We also observe an increase in H2O2 when we overexpress
GO:0005829 cytosol	TAS Reactome:R-HSA-9033235	KEEP AS NON CORE	Summary: Reactome represents a transient cytosolic pre-import pool. Reason: R-HSA-9033235 places PEX5 cargo before release into the matrix. Retain this transport-context localization without making cytosol an additional catalytic compartment for mature ACOX1. Supporting Evidence: Reactome:R-HSA-9033235 the cargo protein is released into the peroxisomal matrix
GO:0005829 cytosol	TAS Reactome:R-HSA-9033236	KEEP AS NON CORE	Summary: The docking reaction represents cargo before matrix entry. Reason: R-HSA-9033236 concerns cargo-bound PEX5 binding the peroxisomal docking/translocation machinery. This is consistent with a transient cytosolic pool of newly synthesized ACOX1, rather than evidence for a separate cytosolic oxidase role. Supporting Evidence: Reactome:R-HSA-9033236 PEX5S or PEX5L bound to cargo proteins containing PTS1 interacts with the Docking and Translocation Module (PEX13:PEX14:PEX2:PEX10:PEX12)
GO:0005782 peroxisomal matrix	TAS Reactome:R-HSA-9033235	ACCEPT	Summary: The matrix is the destination and catalytic compartment of ACOX1. Reason: The original Reactome cargo-translocation reaction explicitly releases cargo into the matrix. Human PTS1 targeting and independent peroxisomal localization corroborate this location. Supporting Evidence: Reactome:R-HSA-9033235 the cargo protein is released into the peroxisomal matrix PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal
GO:0016020 membrane	HDA PMID:19946888 Defining the membrane proteome of NK cells.	UNDECIDED	Summary: The NK-cell membrane-proteome annotation remains unresolved. Reason: The accessible PMID:19946888 abstract describes YTS NK-like-cell membrane fractionation and proteins predicted to associate transiently with membranes. Its aggregate prediction percentages do not identify which fraction contained ACOX1 or distinguish a peripheral association from carryover for this protein. The ACOX1-specific peptide evidence, treatment behavior and localization controls remain inaccessible. Retain UNDECIDED because the experimental assertion is unresolved; soluble peroxisomal-matrix localization alone does not contradict membrane association. Supporting Evidence: PMID:19946888 The remaining species were largely involved in cellular processes and molecular functions that could be predicted to be transiently associated with membranes.
GO:0030165 PDZ domain binding	IDA PMID:23209302 KIF14 negatively regulates Rap1a-Radil signaling during brea...	UNDECIDED	Summary: ACOX1 is included in the Radil interaction figure; the specific PDZ-binding claim remains unresolved. Reason: The externally retrieved primary JCB PDF Figure 3B contains ACOX1 in the FLAG-mRadil/FLAG-mRadilΔPDZ proteomic screen, although its name is absent from the cached body text. The relevant heat-map colors and supplementary Table S2 were not readable in this session, so no ACOX1 wild-type/deletion contrast is inferred. Affinity purification alone would not establish direct PDZ-domain recognition. Figure 1 directly tests KIF14, a different interactor. The published Radil motif [FI]-[FWT]-WV is not the ACOX1 terminal SKL; this does not rule out noncanonical binding. Supporting Evidence: PMID:23209302 Shown is a protein–protein interaction heat map for FLAG-mRadil and FLAG-mRadilΔPDZ.
GO:0005782 peroxisomal matrix	TAS Reactome:R-HSA-1989749	ACCEPT	Summary: Retain the matrix location in the ACOX1 expression event. Reason: R-HSA-1989749 is a curated expression event, not an independent localization assay. Its matrix assignment agrees with PTS1-dependent targeting and the enzyme reaction compartment. Supporting Evidence: PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal PMID:32169171 both hACOX1WT and hACOX1N237S are localized to peroxisomes
GO:0005782 peroxisomal matrix	TAS Reactome:R-HSA-2066787	ACCEPT	Summary: Retain the peroxisomal matrix location of the DHA precursor oxidation step. Reason: R-HSA-2066787 describes the ACOX1-catalyzed initial oxidation during C24:6(n-3) retroconversion. The cached reaction title says tetracosapentaenoyl, whereas its summary specifies C24:6; preserve the source title and derive the chemistry from the reaction summary. The annotation being reviewed is the matrix location. Supporting Evidence: Reactome:R-HSA-2066787 This step is catalysed by the peroxisomal enzyme Straight-chain acyl-CoA oxidase (SCOX) PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal
GO:0005782 peroxisomal matrix	TAS Reactome:R-HSA-390256	ACCEPT	Summary: Retain the matrix location of C26:0-CoA oxidation. Reason: R-HSA-390256 assigns ACOX1 to the peroxisomal C26:0-CoA oxidation reaction. This pathway localization is consistent with human PTS1 targeting and VLCFA deficiency evidence. Supporting Evidence: PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal PMID:18536048 Studies in fibroblasts from the two patients revealed a deficiency of one of the two peroxisomal acyl-CoA oxidases, that is, straight-chain acyl-CoA oxidase (ACOX1).
GO:0005777 peroxisome	IDA PMID:8943006 Molecular characterization of the human peroxisomal branched...	ACCEPT	Summary: The peroxisomal location is independently established. Reason: PMID:8943006 foregrounds branched-chain ACOX2 but explicitly distinguishes the peroxisomal palmitoyl-CoA oxidase. Its ACOX1-specific full experimental localization detail was unavailable. Defer to the original IDA curator and accept using independent human ACOX1 localization; do not infer misattribution from the title. Supporting Evidence: PMID:32169171 both hACOX1WT and hACOX1N237S are localized to peroxisomes PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal
GO:0005777 peroxisome	IDA PMID:17881773 Peroxisomes in human and mouse testis: differential expressi...	ACCEPT	Summary: Retain the experimentally curated peroxisomal location. Reason: The accessible PMID:17881773 abstract studies human and mouse testicular peroxisomal proteins but does not resolve the ACOX1-specific experiment. The original curator had the full paper; independent human ACOX1 localization and PTS1 evidence establish the location without inventing testis-specific assay details. Supporting Evidence: PMID:32169171 both hACOX1WT and hACOX1N237S are localized to peroxisomes PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal
GO:0000038 very long-chain fatty acid metabolic process	IMP PMID:18536048 Peroxisomal acyl-CoA-oxidase deficiency: two new cases.	ACCEPT	Summary: Patient evidence connects ACOX1 deficiency with abnormal VLCFA metabolism. Reason: The two cases have abnormal plasma VLCFAs and deficient straight-chain acyl-CoA oxidase in fibroblasts. Together with direct catalytic chemistry, this supports the human metabolic annotation. Supporting Evidence: PMID:18536048 Plasma very-long-chain fatty acids were abnormal in both patients PMID:18536048 Studies in fibroblasts from the two patients revealed a deficiency of one of the two peroxisomal acyl-CoA oxidases, that is, straight-chain acyl-CoA oxidase (ACOX1).
GO:0003997 acyl-CoA oxidase activity	IMP PMID:18536048 Peroxisomal acyl-CoA-oxidase deficiency: two new cases.	ACCEPT	Summary: Patient fibroblasts are deficient in ACOX1 enzyme activity. Reason: The accessible original abstract explicitly identifies straight-chain acyl-CoA oxidase deficiency. Preserve the IMP evidence as perturbational support for the known catalytic function. Supporting Evidence: PMID:18536048 Studies in fibroblasts from the two patients revealed a deficiency of one of the two peroxisomal acyl-CoA oxidases, that is, straight-chain acyl-CoA oxidase (ACOX1).
GO:0033540 fatty acid beta-oxidation using acyl-CoA oxidase	IMP PMID:18536048 Peroxisomal acyl-CoA-oxidase deficiency: two new cases.	ACCEPT	Summary: Human enzyme deficiency supports the oxidase-dependent beta-oxidation pathway. Reason: ACOX1-deficient fibroblasts and abnormal plasma VLCFAs support the disease pathway; recombinant enzyme chemistry identifies ACOX1 as performing the initial oxidative step, not merely regulating the process. Supporting Evidence: PMID:18536048 Studies in fibroblasts from the two patients revealed a deficiency of one of the two peroxisomal acyl-CoA oxidases, that is, straight-chain acyl-CoA oxidase (ACOX1). PMID:18536048 Plasma very-long-chain fatty acids were abnormal in both patients PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0005515 protein binding	IPI PMID:18281296 Contribution of peroxisome-specific isoform of Lon protease ...	REMOVE	Summary: The LONP2 association does not supply an informative ACOX1 molecular-function term. Reason: Remove generic protein binding under the project policy, not because the reported co-immunoprecipitation is false. The accessible original abstract supports association and impaired AOX processing with dominant-negative pLon, but reports little if any in-vitro processing by pLon itself. A direct LONP2 activation mechanism is therefore not established, and being a processing client does not justify an invented adapter or protease function for ACOX1. Supporting Evidence: PMID:18281296 Proteomic analysis of proteins co-immunoprecipitated with Lon suggested that Lon interacts with PMP70 and several enzymes involved in beta-oxidation, including acyl-CoA oxidase (AOX). PMID:18281296 pLon exhibits little, if any, in vitro AOX processing activity
GO:0003997 acyl-CoA oxidase activity	IMP PMID:7876265 Overexpression and characterization of the human peroxisomal...	ACCEPT	Summary: Purified recombinant human ACOX1 has palmitoyl-CoA oxidase activity. Reason: The original human-enzyme study provides activity and kinetic measurements, directly supporting the molecular function. The full-length A component and complementary B/C fragments were also compared; this is not only a sequence inference. Supporting Evidence: PMID:7876265 Using the purified enzyme, Km and Vmax values for palmitoyl-CoA were found to be 10 microM and 1.4 units/mg of protein, respectively. PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0003997 acyl-CoA oxidase activity	IDA PMID:8117268 Molecular cloning and functional expression of a human perox...	ACCEPT	Summary: Cloned human ACOX1 is enzymatically active. Reason: PMID:8117268 reports functional expression of the human cDNA in fibroblasts and catalytically active AOX. This directly supports the seeded IDA. Supporting Evidence: PMID:8117268 the expressed AOX was catalytically active
GO:0005777 peroxisome	IDA PMID:7876265 Overexpression and characterization of the human peroxisomal...	ACCEPT	Summary: Accept peroxisomal localization with independent corroboration. Reason: The available PMID:7876265 abstract emphasizes insect-cell overexpression, including cytoplasmic particles, and does not expose the exact experiment behind the original localization IDA. Do not recast the insect expression pattern as endogenous human localization. Retain the curator assertion using independent human PTS1 and colocalization evidence. Supporting Evidence: PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal PMID:32169171 both hACOX1WT and hACOX1N237S are localized to peroxisomes
GO:0005777 peroxisome	IDA PMID:8117268 Molecular cloning and functional expression of a human perox...	ACCEPT	Summary: The human protein has an SKL targeting signal and peroxisome-dependent accumulation. Reason: The cloned protein terminates in PTS1 and accumulates poorly in Zellweger fibroblasts lacking normal peroxisomes. Alongside the original curator interpretation and later colocalization, this supports the peroxisomal assignment. Supporting Evidence: PMID:8117268 including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal PMID:8117268 while only a limited amount was found in Zellweger syndrome patient's fibroblast not having normal peroxisomes. PMID:32169171 both hACOX1WT and hACOX1N237S are localized to peroxisomes
GO:0006091 generation of precursor metabolites and energy	IMP PMID:7876265 Overexpression and characterization of the human peroxisomal...	KEEP AS NON CORE	Summary: Retain the broad precursor-metabolite role alongside the defined oxidase pathway. Reason: GO:0006091 includes pathways that form precursor metabolites and is not restricted to direct ATP synthesis. PMID:7876265 demonstrates active recombinant human ACOX1 catalyzing the initial straight-chain acyl-CoA oxidation reaction, establishing direct participation in a pathway that generates shorter-chain metabolites. Retain the broad experimental annotation as non-core with this pathway interpretation and curator deference, without claiming that ACOX1 itself generates ATP or releases acetyl-CoA. The displayed AmiGO is_a ancestry of GO:0006635 does not include GO:0006091, so replacing this row with beta-oxidation would not simply refine an established parent-child relation. Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0006629 lipid metabolic process	IDA PMID:8117268 Molecular cloning and functional expression of a human perox...	MODIFY	Summary: Refine lipid metabolism to fatty-acid beta-oxidation. Reason: The expressed human protein is catalytically active AOX. Its defined oxidative role supports the specific process term; the broad lipid-process annotation is correct but less informative. Proposed replacements: fatty acid beta-oxidation Supporting Evidence: PMID:8117268 the expressed AOX was catalytically active PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0006693 prostaglandin metabolic process	IMP PMID:7876265 Overexpression and characterization of the human peroxisomal...	KEEP AS NON CORE	Summary: Prostaglandin-CoA oxidation is a documented part of the substrate range. Reason: The original human enzyme characterization explicitly includes prostaglandin CoA esters. Retain this substrate-linked metabolic role as non-core relative to the integrated fatty-acyl-CoA oxidase function; the accessible abstract does not quantify its physiological flux or establish that it is evolutionarily minor. Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.
GO:0019395 fatty acid oxidation	IMP PMID:7876265 Overexpression and characterization of the human peroxisomal...	ACCEPT	Summary: ACOX1 directly performs fatty-acid oxidation. Reason: Recombinant human enzyme oxidizes fatty-acyl-CoA substrates with oxygen as acceptor. This is the catalytic step itself, so the original process annotation is supported. Supporting Evidence: PMID:7876265 The palmitoyl-CoA oxidase (ACOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2.

Gene Description

Existing Annotations Review

Core Functions

References

📚 Additional Documentation

Notes

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