Ddo

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005782 peroxisomal matrix	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: The peroxisomal matrix annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0006531 aspartate metabolic process	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: The aspartate metabolic process annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The annotation is compatible with Ddo biology but is broader or more contextual than the core molecular function. Supporting Evidence: UniProtKB:D3ZDM7 Suppresses the level of D-aspartate in the brain
GO:0008445 D-aspartate oxidase activity	IBA GO_REF:0000033	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-aspartate oxidase activity annotation is supported by the fetched UniProt/GOA evidence (IBA, GO_REF:0000033) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+) file:rat/Ddo/Ddo-deep-research-falcon.md Ddo/DDO (D-aspartate oxidase; EC 1.4.3.1) is an FAD-containing flavoprotein that catalyzes oxidative deamination of acidic D-amino acids to yield the corresponding 2-oxo acid, hydrogen peroxide (H2O2), and ammonia (NH3) file:rat/Ddo/Ddo-deep-research-falcon.md In the case of D-Asp, the 2-oxo acid product is oxaloacetate
GO:0019478 D-amino acid catabolic process	IBA GO_REF:0000033	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-amino acid catabolic process annotation is supported by the fetched UniProt/GOA evidence (IBA, GO_REF:0000033) and represents a core or direct activity/process. Falcon deep research corroborates that DDO-mediated catabolism is the dominant in vivo control point for D-aspartate levels. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: UniProtKB:D3ZDM7 Protects the organism from the toxicity of D-amino acids file:rat/Ddo/Ddo-deep-research-falcon.md Ddo knockout is associated with ~10–20× higher brain D-Asp in multiple regions, demonstrating that DDO-mediated catabolism strongly limits steady-state D-Asp
GO:0003884 D-amino-acid oxidase activity	IEA GO_REF:0000002	MODIFY	Summary: The D-amino-acid oxidase activity annotation is related to Ddo function, but it is too generic compared with the supported specific term(s): D-aspartate oxidase activity. Reason: The annotation is directionally related to Ddo but is too broad; the specific catalytic activity is more informative. Proposed replacements: D-aspartate oxidase activity Supporting Evidence: UniProtKB:D3ZDM7 FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids file:rat/Ddo/Ddo-deep-research-falcon.md Ddo is not a broad-spectrum D-amino acid oxidase (DAO-like), but rather a specialized enzyme controlling the pool of acidic D-amino acids
GO:0005782 peroxisomal matrix	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: The peroxisomal matrix annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0005829 cytosol	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: The cytosol annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: UniProtKB:D3ZDM7 Cytoplasm, cytosol {ECO:0000250\|UniProtKB:Q99489}
GO:0008445 D-aspartate oxidase activity	IEA GO_REF:0000120	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-aspartate oxidase activity annotation is supported by the fetched UniProt/GOA evidence (IEA, GO_REF:0000120) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0046416 D-amino acid metabolic process	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: The D-amino acid metabolic process annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The annotation is compatible with Ddo biology but is broader or more contextual than the core molecular function. GOA no longer carries this InterPro-based row. Supporting Evidence: UniProtKB:D3ZDM7 FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids
GO:0071949 FAD binding	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: The FAD binding annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Falcon deep research confirms DDO is an FAD-dependent flavoenzyme whose catalysis requires the bound FAD cofactor. Reason: This is plausible biochemical context for Ddo, but it is not the defining evolved activity. Supporting Evidence: UniProtKB:D3ZDM7 Name=FAD; Xref=ChEBI:CHEBI:57692; file:rat/Ddo/Ddo-deep-research-falcon.md DDO is an FAD-dependent flavoenzyme, and experimental recombinant preparations and assays include FAD, consistent with tight cofactor dependence
GO:0005777 peroxisome	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: The peroxisome annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0010646 regulation of cell communication	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: The regulation of cell communication annotation likely reflects indirect phenotype, expression, or pathway context rather than the direct conserved function of Ddo. Reason: This phenotype or tissue/developmental term overstates the direct functional role of Ddo; it is better treated as downstream context. Supporting Evidence: UniProtKB:D3ZDM7 Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity).
GO:0019478 D-amino acid catabolic process	IEA GO_REF:0000120	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-amino acid catabolic process annotation is supported by the fetched UniProt/GOA evidence (IEA, GO_REF:0000120) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: UniProtKB:D3ZDM7 Protects the organism from the toxicity of D-amino acids
GO:0050877 nervous system process	IEA GO_REF:0000120	MARK AS OVER ANNOTATED	Summary: The nervous system process annotation likely reflects indirect phenotype, expression, or pathway context rather than the direct conserved function of Ddo. Falcon deep research clarifies that any neural effect is mediated indirectly through DDO control of D-aspartate, which in turn modulates NMDA-receptor/glutamatergic signaling; the direct molecular activity remains acidic D-amino-acid oxidation, so this process term is best treated as downstream context. Reason: This phenotype or tissue/developmental term overstates the direct functional role of Ddo; it is better treated as downstream context. Supporting Evidence: UniProtKB:D3ZDM7 Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity). file:rat/Ddo/Ddo-deep-research-falcon.md D-Asp can stimulate NMDA receptors by binding the L-glutamate site, and DDO therefore indirectly modulates glutamatergic neurotransmission through D-Asp availability
GO:0005829 cytosol	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: The cytosol annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: UniProtKB:D3ZDM7 Cytoplasm, cytosol {ECO:0000250\|UniProtKB:Q99489}
GO:0005782 peroxisomal matrix	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: The peroxisomal matrix annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0005782 peroxisomal matrix	EXP PMID:12209855 Cellular and subcellular distribution of D-aspartate oxidase...	KEEP AS NON CORE	Summary: The peroxisomal matrix annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: PMID:12209855 Immunoelectron microscopy showed that the protein is localized in single membrane-bound organelles, apparently peroxisomes. UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0005782 peroxisomal matrix	EXP PMID:1991137 D-aspartate oxidase, a peroxisomal enzyme in liver of rat an...	KEEP AS NON CORE	Summary: The peroxisomal matrix annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: PMID:1991137 By means of subcellular fractionation D-aspartate oxidase was shown to be localized in peroxisomes in rat and human liver. UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0008445 D-aspartate oxidase activity	ISO GO_REF:0000121	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-aspartate oxidase activity annotation is supported by the fetched UniProt/GOA evidence (ISO, GO_REF:0000121) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0008445 D-aspartate oxidase activity	EXP PMID:32376478 Biochemical characterization of d-aspartate oxidase from Cae...	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-aspartate oxidase activity annotation is supported by the fetched UniProt/GOA evidence (EXP, PMID:32376478) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: PMID:32376478 C. elegans DDO-1, but not mammalian (rat) DDO, efficiently and selectively degraded d-glutamate in addition to d-aspartate UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0047821 D-glutamate oxidase activity	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: D-glutamate is a genuine, acidic D-amino-acid substrate of DDO, although it is a much weaker substrate than D-aspartate. The rat UniProt record lists D-glutamate oxidation (RHEA:10028) as a catalytic activity by similarity, and falcon deep research confirms DDO is selective for acidic D-amino acids classically including D-glutamate. This is therefore a real but minor (non-core) activity rather than an over-annotation; the prior MARK_AS_OVER_ANNOTATED reasoning ("no activity") conflated the much lower turnover of D-glutamate with absence of activity. Reason: D-glutamate is a bona fide but minor acidic D-amino-acid substrate of DDO; it is supported by similarity but is not the defining/core activity, which is D-aspartate oxidation. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-glutamate + O2 + H2O = 2-oxoglutarate + H2O2 + NH4(+); file:rat/Ddo/Ddo-deep-research-falcon.md DDO is highly selective for acidic D-amino acids, classically D-Asp and D-glutamate (D-Glu)
GO:0047821 D-glutamate oxidase activity	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: D-glutamate is a genuine, acidic D-amino-acid substrate of DDO, although it is a much weaker substrate than D-aspartate. The rat UniProt record lists D-glutamate oxidation (RHEA:10028) as a catalytic activity by similarity, and falcon deep research confirms DDO acts on acidic D-amino acids beyond D-aspartate (e.g. D-Glu at ~12.8% of D-Asp activity). This is a real but minor (non-core) activity rather than an over-annotation. Reason: D-glutamate is a bona fide but minor acidic D-amino-acid substrate of DDO; it is supported by similarity but is not the defining/core activity, which is D-aspartate oxidation. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-glutamate + O2 + H2O = 2-oxoglutarate + H2O2 + NH4(+); file:rat/Ddo/Ddo-deep-research-falcon.md 7.82 ± 1.39 µmol/min/mg; ~12.8% of D-Asp activity in another study
GO:0005782 peroxisomal matrix	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: The peroxisomal matrix annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0005777 peroxisome	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: The peroxisome annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0008445 D-aspartate oxidase activity	IDA PMID:29292239 Rat d-aspartate oxidase is more similar to the human enzyme ...	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-aspartate oxidase activity annotation is supported by the fetched UniProt/GOA evidence (IDA, PMID:29292239) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: PMID:29292239 the structural and enzymatic properties of purified recombinant rat, mouse and human DDOs were examined and compared UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0019478 D-amino acid catabolic process	ISO GO_REF:0000121	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-amino acid catabolic process annotation is supported by the fetched UniProt/GOA evidence (ISO, GO_REF:0000121) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: UniProtKB:D3ZDM7 Protects the organism from the toxicity of D-amino acids
GO:0071949 FAD binding	IDA PMID:32376478 Biochemical characterization of d-aspartate oxidase from Cae...	KEEP AS NON CORE	Summary: The FAD binding annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: This is plausible biochemical context for Ddo, but it is not the defining evolved activity. Supporting Evidence: PMID:32376478 d-Aspartate oxidase (DDO) is a flavin adenine dinucleotide (FAD)-containing flavoprotein that stereospecifically acts on acidic d-amino acids UniProtKB:D3ZDM7 Name=FAD; Xref=ChEBI:CHEBI:57692;
GO:0005777 peroxisome	IDA PMID:12209855 Cellular and subcellular distribution of D-aspartate oxidase...	KEEP AS NON CORE	Summary: The peroxisome annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Falcon deep research corroborates the peroxisomal localization and notes it positions DDO as a source of peroxisomal H2O2. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: PMID:12209855 Immunoelectron microscopy showed that the protein is localized in single membrane-bound organelles, apparently peroxisomes. UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix. file:rat/Ddo/Ddo-deep-research-falcon.md peroxisomal localization positions DDO as a source of peroxisomal H2O2, linking Ddo activity not only to D-Asp turnover but also potentially to redox signaling/oxidative stress microdomains, depending on tissue context
GO:0019478 D-amino acid catabolic process	IDA PMID:29292239 Rat d-aspartate oxidase is more similar to the human enzyme ...	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-amino acid catabolic process annotation is supported by the fetched UniProt/GOA evidence (IDA, PMID:29292239) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: PMID:29292239 the structural and enzymatic properties of purified recombinant rat, mouse and human DDOs were examined and compared UniProtKB:D3ZDM7 Protects the organism from the toxicity of D-amino acids
GO:0071949 FAD binding	IDA PMID:29292239 Rat d-aspartate oxidase is more similar to the human enzyme ...	KEEP AS NON CORE	Summary: The FAD binding annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: This is plausible biochemical context for Ddo, but it is not the defining evolved activity. Supporting Evidence: PMID:29292239 the structural and enzymatic properties of purified recombinant rat, mouse and human DDOs were examined and compared UniProtKB:D3ZDM7 Name=FAD; Xref=ChEBI:CHEBI:57692;
GO:0005777 peroxisome	IDA PMID:1991137 D-aspartate oxidase, a peroxisomal enzyme in liver of rat an...	KEEP AS NON CORE	Summary: The peroxisome annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The localization is useful context but is not the core molecular function of Ddo. Supporting Evidence: PMID:1991137 By means of subcellular fractionation D-aspartate oxidase was shown to be localized in peroxisomes in rat and human liver. UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0008445 D-aspartate oxidase activity	IDA PMID:25747990 Characterization of the enzymatic and structural properties ...	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-aspartate oxidase activity annotation is supported by the fetched UniProt/GOA evidence (IDA, PMID:25747990) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: PMID:25747990 The kinetic and inhibitor-binding properties of this enzyme were also compared with those of purified recombinant rat and mouse DDOs. UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0019478 D-amino acid catabolic process	IDA PMID:25747990 Characterization of the enzymatic and structural properties ...	ACCEPT	Summary: Ddo is a D-aspartate oxidase; the D-amino acid catabolic process annotation is supported by the fetched UniProt/GOA evidence (IDA, PMID:25747990) and represents a core or direct activity/process. Reason: This term captures a directly supported part of Ddo core biochemistry or the closest GO process for that activity. Supporting Evidence: PMID:25747990 The kinetic and inhibitor-binding properties of this enzyme were also compared with those of purified recombinant rat and mouse DDOs. UniProtKB:D3ZDM7 Protects the organism from the toxicity of D-amino acids
GO:0010646 regulation of cell communication	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: The regulation of cell communication annotation likely reflects indirect phenotype, expression, or pathway context rather than the direct conserved function of Ddo. Reason: This phenotype or tissue/developmental term overstates the direct functional role of Ddo; it is better treated as downstream context. Propagation Review Root cause: PROPAGATION BAD Failure modes: CONTEXT OR TISSUE MISMATCH Sources checked: MGI:MGI:1925528 · mouse Ddo SUPPORTS SOURCE BUT NOT TARGET Mouse donor support is IMP evidence from Ddo-knockout studies (PMID:26961959, PMID:35915065); a downstream consequence of raised D-aspartate rather than a direct molecular role. Supporting Evidence: UniProtKB:D3ZDM7 Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity).
GO:0050877 nervous system process	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: The nervous system process annotation likely reflects indirect phenotype, expression, or pathway context rather than the direct conserved function of Ddo. Reason: This phenotype or tissue/developmental term overstates the direct functional role of Ddo; it is better treated as downstream context. Propagation Review Root cause: PROPAGATION BAD Failure modes: CONTEXT OR TISSUE MISMATCH Sources checked: UniProtKB:Q99489 · human DDO SUPPORTS SOURCE BUT NOT TARGET Human DDO donor evidence is an IMP (PMID:28560262) about neurological consequences of impaired D-aspartate degradation; phenotype-level context rather than enzyme function. MGI:MGI:1925528 · mouse Ddo SUPPORTS SOURCE BUT NOT TARGET Mouse donor rows are knockout IMPs (PMID:26961959, PMID:35915065) carrying the same phenotype-level caveat. Supporting Evidence: UniProtKB:D3ZDM7 Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity).
GO:0071949 FAD binding	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: The FAD binding annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: This is plausible biochemical context for Ddo, but it is not the defining evolved activity. Supporting Evidence: UniProtKB:D3ZDM7 Name=FAD; Xref=ChEBI:CHEBI:57692;
GO:0006533 L-aspartate catabolic process	ISO GO_REF:0000121	REMOVE	Summary: Ddo is a D-aspartate oxidase that is stereospecific for acidic D-amino acids; the L-aspartate catabolic process transfer is contradicted by the enzyme's substrate specificity. Reason: DDO is stereospecific for D-aspartate (and other acidic D-amino acids) and acts on the D-enantiomer only; it does not oxidize L-aspartate, so a role in L-aspartate catabolism is contradicted rather than merely broad. The human donor (DDO, Q99489 and isoform Q99489-1) does not carry this term on its canonical record in QuickGO, so the source cannot be traced. Changed from MARK_AS_OVER_ANNOTATED to REMOVE because the claim is wrong, not just overstated. Propagation Review Root cause: SOURCE STALE OR MISSING Sources checked: UniProtKB:Q99489 · human DDO SOURCE STALE OR MISSING The canonical human DDO record in QuickGO carries no L-aspartate catabolic process annotation, and isoform-level tracing (Q99489-1) did not recover a source; the claim also conflicts with DDO's stereospecificity for D-aspartate. Supporting Evidence: PMID:29292239 d-Aspartate oxidase (DDO) is a degradative enzyme that is stereospecific for the acidic amino acid d-aspartate UniProtKB:D3ZDM7 FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids
GO:0006531 aspartate metabolic process	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: The aspartate metabolic process annotation is plausible for Ddo but should be kept as non-core context rather than used to define the gene product function. Reason: The annotation is compatible with Ddo biology but is broader or more contextual than the core molecular function. Supporting Evidence: UniProtKB:D3ZDM7 Suppresses the level of D-aspartate in the brain
GO:0007320 insemination	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: The insemination annotation likely reflects indirect phenotype, expression, or pathway context rather than the direct conserved function of Ddo. Reason: This phenotype or tissue/developmental term overstates the direct functional role of Ddo; it is better treated as downstream context. Propagation Review Root cause: PROPAGATION BAD Failure modes: CONTEXT OR TISSUE MISMATCH Sources checked: MGI:MGI:1925528 · mouse Ddo SUPPORTS SOURCE BUT NOT TARGET Mouse donor support is an IMP from Ddo-knockout reproductive phenotyping (PMID:16525061); an organismal outcome of altered D-aspartate levels. Supporting Evidence: UniProtKB:D3ZDM7 FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids
GO:0007625 grooming behavior	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: The grooming behavior annotation likely reflects indirect phenotype, expression, or pathway context rather than the direct conserved function of Ddo. Reason: This phenotype or tissue/developmental term overstates the direct functional role of Ddo; it is better treated as downstream context. Propagation Review Root cause: PROPAGATION BAD Failure modes: CONTEXT OR TISSUE MISMATCH Sources checked: MGI:MGI:1925528 · mouse Ddo SUPPORTS SOURCE BUT NOT TARGET Mouse donor support is an IMP from knockout behavioural phenotyping (PMID:16525061), not a molecular role of the oxidase. Supporting Evidence: UniProtKB:D3ZDM7 FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids
GO:0042445 hormone metabolic process	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: The hormone metabolic process annotation likely reflects indirect phenotype, expression, or pathway context rather than the direct conserved function of Ddo. Reason: This phenotype or tissue/developmental term overstates the direct functional role of Ddo; it is better treated as downstream context. Propagation Review Root cause: PROPAGATION BAD Failure modes: CONTEXT OR TISSUE MISMATCH Sources checked: MGI:MGI:1925528 · mouse Ddo SUPPORTS SOURCE BUT NOT TARGET Mouse donor support is an IMP from the same knockout study (PMID:16525061) linking D-aspartate to hormone levels; an indirect consequence of substrate degradation. Supporting Evidence: UniProtKB:D3ZDM7 FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids
GO:0005777 peroxisome	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: Peroxisome transferred by orthology from the ortholog record RGD:14215375; donor-split duplicate of an existing ISO row for the same term. Reason: DDO is a peroxisomal-matrix enzyme in human and rat (rat EXP/IDA rows, PMID:1991137 and PMID:12209855); the localization transfers correctly but is context rather than the defining activity. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0005777 peroxisome	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: Peroxisome transferred by orthology from human DDO (UniProtKB:Q99489); donor-split duplicate of an existing ISO row for the same term. Reason: DDO is a peroxisomal-matrix enzyme in human and rat (rat EXP/IDA rows, PMID:1991137 and PMID:12209855); the localization transfers correctly but is context rather than the defining activity. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0005777 peroxisome	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: Peroxisome transferred by orthology from human DDO and its isoform 1 (UniProtKB:Q99489, Q99489-1); donor-split duplicate of an existing ISO row for the same term. Reason: DDO is a peroxisomal-matrix enzyme in human and rat (rat EXP/IDA rows, PMID:1991137 and PMID:12209855); the localization transfers correctly but is context rather than the defining activity. Supporting Evidence: UniProtKB:D3ZDM7 Note=Active in the peroxisomal matrix.
GO:0008445 D-aspartate oxidase activity	ISO GO_REF:0000121	ACCEPT	Summary: D-aspartate oxidase activity transferred by orthology from the ortholog record RGD:14215375; donor-split duplicate of an existing ISO row for the same term. Reason: D-aspartate oxidase activity is the defining, conserved activity of DDO and is directly demonstrated for recombinant rat DDO (IDA/EXP rows); the transfer is sound. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0008445 D-aspartate oxidase activity	ISO GO_REF:0000121	ACCEPT	Summary: D-aspartate oxidase activity transferred by orthology from human DDO (UniProtKB:Q99489); donor-split duplicate of an existing ISO row for the same term. Reason: D-aspartate oxidase activity is the defining, conserved activity of DDO and is directly demonstrated for recombinant rat DDO (IDA/EXP rows); the transfer is sound. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0008445 D-aspartate oxidase activity	ISO GO_REF:0000121	ACCEPT	Summary: D-aspartate oxidase activity transferred by orthology from human DDO and its isoform 1 (UniProtKB:Q99489, Q99489-1); donor-split duplicate of an existing ISO row for the same term. Reason: D-aspartate oxidase activity is the defining, conserved activity of DDO and is directly demonstrated for recombinant rat DDO (IDA/EXP rows); the transfer is sound. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0008445 D-aspartate oxidase activity	ISO GO_REF:0000121	ACCEPT	Summary: D-aspartate oxidase activity transferred by orthology from human DDO and its isoforms 1 and 3 (UniProtKB:Q99489, Q99489-1, Q99489-3); donor-split duplicate of an existing ISO row for the same term. Reason: D-aspartate oxidase activity is the defining, conserved activity of DDO and is directly demonstrated for recombinant rat DDO (IDA/EXP rows); the transfer is sound. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-aspartate + O2 + H2O = oxaloacetate + H2O2 + NH4(+)
GO:0019478 D-amino acid catabolic process	ISO GO_REF:0000121	ACCEPT	Summary: D-amino acid catabolic process transferred by orthology from the ortholog record RGD:14215375; donor-split duplicate of an existing ISO row for the same term. Reason: DDO catalyses the degradative oxidation of D-aspartate, directly performing D-amino acid catabolism; supported for rat by IDA rows and the transfer is sound. Supporting Evidence: UniProtKB:D3ZDM7 Protects the organism from the toxicity of D-amino acids
GO:0019478 D-amino acid catabolic process	ISO GO_REF:0000121	ACCEPT	Summary: D-amino acid catabolic process transferred by orthology from human DDO (UniProtKB:Q99489); donor-split duplicate of an existing ISO row for the same term. Reason: DDO catalyses the degradative oxidation of D-aspartate, directly performing D-amino acid catabolism; supported for rat by IDA rows and the transfer is sound. Supporting Evidence: UniProtKB:D3ZDM7 Protects the organism from the toxicity of D-amino acids
GO:0019478 D-amino acid catabolic process	ISO GO_REF:0000121	ACCEPT	Summary: D-amino acid catabolic process transferred by orthology from human DDO and its isoforms 1 and 3 (UniProtKB:Q99489, Q99489-1, Q99489-3); donor-split duplicate of an existing ISO row for the same term. Reason: DDO catalyses the degradative oxidation of D-aspartate, directly performing D-amino acid catabolism; supported for rat by IDA rows and the transfer is sound. Supporting Evidence: UniProtKB:D3ZDM7 Protects the organism from the toxicity of D-amino acids
GO:0047821 D-glutamate oxidase activity	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: D-glutamate oxidase activity transferred by orthology from the ortholog record RGD:14215375; donor-split duplicate of an existing ISO row for the same term. Reason: D-glutamate is a genuine but much weaker substrate of mammalian DDO than D-aspartate; consistent with the other D-glutamate oxidase rows it is kept as a non-core activity. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-glutamate + O2 + H2O = 2-oxoglutarate + H2O2 + NH4(+)
GO:0047821 D-glutamate oxidase activity	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: D-glutamate oxidase activity transferred by orthology from human DDO (UniProtKB:Q99489); donor-split duplicate of an existing ISO row for the same term. Reason: D-glutamate is a genuine but much weaker substrate of mammalian DDO than D-aspartate; consistent with the other D-glutamate oxidase rows it is kept as a non-core activity. Supporting Evidence: UniProtKB:D3ZDM7 Reaction=D-glutamate + O2 + H2O = 2-oxoglutarate + H2O2 + NH4(+)
GO:0050877 nervous system process	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: Nervous system process transferred by orthology from human DDO (UniProtKB:Q99489); donor-split of the mouse-donor ISO row for the same term. Reason: DDO affects neural function only indirectly, by degrading D-aspartate, an NMDA-receptor agonist. A broad organismal nervous system process overstates the enzyme's direct role, as for the sibling rows for this term. Propagation Review Root cause: PROPAGATION BAD Failure modes: CONTEXT OR TISSUE MISMATCH Sources checked: UniProtKB:Q99489 · human DDO SUPPORTS SOURCE BUT NOT TARGET Human DDO donor evidence is an IMP (PMID:28560262) about neurological consequences of impaired D-aspartate degradation; phenotype-level context rather than enzyme function. Supporting Evidence: UniProtKB:D3ZDM7 Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity).
GO:0071949 FAD binding	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: FAD binding transferred by orthology from human DDO (UniProtKB:Q99489); donor-split duplicate of an existing ISO row for the same term. Reason: DDO is an FAD-containing flavoprotein; FAD binding is a cofactor requirement of the core activity, kept as non-core, consistent with the other FAD binding rows. Supporting Evidence: UniProtKB:D3ZDM7 Name=FAD; Xref=ChEBI:CHEBI:57692;

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

Falcon

📚 Additional Documentation

Notes

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