id: Q96EY8
gene_symbol: MMAB
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  MMAB is the human mitochondrial ATP:cob(I)alamin adenosyltransferase (ATR, cblB),
  a homotrimeric enzyme of the mitochondrial matrix that catalyses the final step of
  adenosylcobalamin (AdoCbl, coenzyme B12) synthesis. It transfers the 5'-deoxyadenosyl
  group from ATP to reduced cob(I)alamin, producing adenosylcob(III)alamin plus inorganic
  triphosphate. Beyond catalysis, MMAB acts as an escort that delivers the newly made AdoCbl
  directly to methylmalonyl-CoA mutase (MMUT/MCM), the AdoCbl-dependent isomerase that converts
  (R)-methylmalonyl-CoA to succinyl-CoA; this hand-off is stimulated by ATP binding to MMAB and
  gated by the cblA G-protein chaperone MMAA. MMAB binds cobalamin in a base-off state and uses
  ATP-organized coordination chemistry to raise the cobalt redox potential and permit reduction
  to cob(I)alamin prior to adenosylation, and it can sacrificially cleave the newly formed
  cobalt-carbon bond to sequester the cofactor as tightly bound cob(II)alamin when the mutase is
  unavailable. Loss-of-function variants cause methylmalonic aciduria, cblB type, an autosomal
  recessive disorder of AdoCbl synthesis that is frequently responsive to vitamin B12.
existing_annotations:
- term:
    id: GO:0008817
    label: corrinoid adenosyltransferase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: >-
      Phylogenetically inferred corrinoid (cob(I)alamin) adenosyltransferase activity, the
      established core molecular function of MMAB. This matches the direct experimental evidence
      and the UniProt catalytic activity assignment (Rhea:56796).
    action: ACCEPT
    reason: >-
      This is the correct core molecular function and is corroborated by multiple independent
      experimental annotations (EXP/IDA) plus the ARBA electronic assignment; the IBA is at the
      right level of specificity.
    supported_by:
    - reference_id: PMID:12514191
      supporting_text: >-
        ATP:cob(I)alamin adenosyltransferase (ATR) catalyzes the terminal step in the conversion
        of cobalamins into Ado-B12.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: >-
      Electronic assignment of mitochondrial localization from the UniProt Subcellular Location
      vocabulary. MMAB carries a cleaved N-terminal mitochondrial transit peptide (residues 1-32)
      and acts in the mitochondrial matrix.
    action: ACCEPT
    reason: >-
      Correct compartment; consistent with the UniProt SUBCELLULAR LOCATION (Mitochondrion), the
      predicted transit peptide, and high-confidence mitochondrial proteomics. The more specific
      matrix location is captured by separate annotations.
    supported_by:
    - reference_id: PMID:33797888
      supporting_text: >-
        In the matrix, adenosyltransferase (ATR, also known as MMAB or CblB) and CblA (or MMAA),
        a G-protein chaperone, are recruited for the synthesis and delivery of AdoCbl to the
        target enzyme, MCM (or Mut)
- term:
    id: GO:0008817
    label: corrinoid adenosyltransferase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: enables
  review:
    summary: >-
      ARBA machine-learning electronic assignment of the core corrinoid adenosyltransferase
      activity, consistent with the experimental and phylogenetic evidence.
    action: ACCEPT
    reason: >-
      Correct core molecular function; the ARBA mapping agrees with EXP/IDA/IBA evidence.
    supported_by:
    - reference_id: PMID:12514191
      supporting_text: >-
        ATP:cob(I)alamin adenosyltransferase (ATR) catalyzes the terminal step in the conversion
        of cobalamins into Ado-B12.
- term:
    id: GO:0009235
    label: cobalamin metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: involved_in
  review:
    summary: >-
      Electronic assignment of involvement in cobalamin metabolism. MMAB performs the terminal step
      of adenosylcobalamin (coenzyme B12) synthesis, so it is correctly placed in cobalamin
      metabolic process.
    action: ACCEPT
    reason: >-
      Correct biological process at an appropriate grain for a human enzyme (humans do not perform
      de novo corrin ring biosynthesis; MMAB acts in cofactor conversion/tailoring of dietary B12).
    supported_by:
    - reference_id: PMID:12514191
      supporting_text: >-
        ATP:cob(I)alamin adenosyltransferase (ATR) catalyzes the terminal step in the conversion
        of cobalamins into Ado-B12.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25910212
  qualifier: enables
  review:
    summary: >-
      Bare protein binding from a large-scale interactome perturbation study (IntAct interactor
      CBY2, Q8NA61-2). Provides no specific information about MMAB molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative generic protein binding derived from a high-throughput screen; the cited paper
      does not characterize MMAB function. Per curation policy, retained but marked as over-annotated
      rather than removed.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32814053
  qualifier: enables
  review:
    summary: >-
      Bare protein binding from a neurodegenerative-disease interactome map (IntAct interactors
      CALR/P27797, DLST/P36957, NEK7/Q8TDX7, OPTN/Q96CV9). Uninformative for molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Generic protein binding from a large-scale two-hybrid/AP-MS network; no functional MMAB
      characterization in the source. Retained but marked as over-annotated per policy.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33961781
  qualifier: enables
  review:
    summary: >-
      Bare protein binding from a proteome-scale interactome network (IntAct interactor DBT/P11182).
      Notably DBT (a mitochondrial 2-oxo acid dehydrogenase E2 subunit) is a plausible matrix
      neighbour, but the annotation itself conveys no specific function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Generic protein binding from a high-throughput interactome; uninformative molecular-function
      term. Retained but marked as over-annotated per policy.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:40205054
  qualifier: enables
  review:
    summary: >-
      Bare protein binding from a multimodal cell-map study (IntAct interactor DBT/P11182).
      Duplicates the DBT interaction and conveys no specific molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Generic protein binding from a large-scale mapping resource; uninformative term. Retained but
      marked as over-annotated per policy.
- term:
    id: GO:0009235
    label: cobalamin metabolic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9759218
  qualifier: involved_in
  review:
    summary: >-
      Reactome-curated involvement of MMAB in cobalamin metabolism, reflecting its role in the
      AdoCbl branch of the intracellular cobalamin trafficking/processing pathway.
    action: ACCEPT
    reason: >-
      Correct biological process, well supported by the enzyme's characterized role in producing
      the AdoCbl cofactor from dietary cobalamin.
    supported_by:
    - reference_id: PMID:33797888
      supporting_text: >-
        Mutations in any of these three proteins lead to isolated methylmalonic aciduria while
        sparing the MeCbl branch of the trafficking pathway.
- term:
    id: GO:0008817
    label: corrinoid adenosyltransferase activity
  evidence_type: EXP
  original_reference_id: PMID:15913339
  qualifier: enables
  review:
    summary: >-
      Experimental (spectroscopic) study of human ATR (MMAB) demonstrating cobalamin binding and the
      ATP-dependent coordination chemistry that underlies its adenosyltransferase function, forming a
      four-coordinate Co2+ cobalamin species that raises the redox potential toward the physiological
      range to enable cob(I)alamin formation prior to adenosylation.
    action: ACCEPT
    reason: >-
      Direct experimental evidence on the human enzyme for its corrinoid adenosyltransferase
      mechanism; supports the core molecular function.
    supported_by:
    - reference_id: PMID:15913339
      supporting_text: >-
        The human adenosyltransferase hATR converts exogenous cobalamin into coenzyme B12 by
        transferring the adenosyl group from cosubstrate ATP to a transiently formed Co1+cobalamin
        (Co1+Cbl) species.
- term:
    id: GO:0008817
    label: corrinoid adenosyltransferase activity
  evidence_type: EXP
  original_reference_id: PMID:30282455
  qualifier: enables
  review:
    summary: >-
      Experimental study confirming that human ATR (MMAB) synthesizes AdoCbl by adenosylation of
      cob(I)alamin by ATP and directly delivers the product to methylmalonyl-CoA mutase; also
      demonstrates the sacrificial Co-C bond homolysis cofactor-conservation activity.
    action: ACCEPT
    reason: >-
      Direct experimental evidence on the human enzyme supporting corrinoid adenosyltransferase
      activity (the AdoCbl-synthesizing reaction).
    supported_by:
    - reference_id: PMID:30282455
      supporting_text: >-
        AdoCbl is synthesized by adenosyltransferase (ATR), which catalyzes the adenosylation of
        cob(I)alamin by ATP in a direct nucleophilic displacement reaction that leads to
        cobalt−carbon (Co−C) bond formation yielding AdoCbl and inorganic triphosphate
- term:
    id: GO:0008817
    label: corrinoid adenosyltransferase activity
  evidence_type: EXP
  original_reference_id: PMID:33797888
  qualifier: enables
  review:
    summary: >-
      Review/primary account (Banerjee lab) describing the human adenosyltransferase (ATR/MMAB)
      homotrimer that catalyses adenosylation of cob(I)alamin by ATP, with detailed loop-dynamics and
      redox-linked coordination chemistry underlying the reaction.
    action: ACCEPT
    reason: >-
      Supports the core corrinoid adenosyltransferase activity of the human enzyme.
    supported_by:
    - reference_id: PMID:33797888
      supporting_text: >-
        ATR, an 81 kDa homotrimer with active sites housed at the subunit interfaces (Fig. 5A),62
        catalyzes the adenosylation of cob(I)alamin by ATP.
- term:
    id: GO:0008817
    label: corrinoid adenosyltransferase activity
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-3322125
  qualifier: enables
  review:
    summary: >-
      Reactome-curated corrinoid adenosyltransferase activity of MMAB, corresponding to the reaction
      MMAB adenosylates cob(I)alamin. Consistent with all experimental evidence.
    action: ACCEPT
    reason: >-
      Correct core molecular function, curated by Reactome and matching the experimental record.
    supported_by:
    - reference_id: PMID:12514191
      supporting_text: >-
        ATP:cob(I)alamin adenosyltransferase (ATR) catalyzes the terminal step in the conversion
        of cobalamins into Ado-B12.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HTP
  original_reference_id: PMID:34800366
  qualifier: located_in
  review:
    summary: >-
      High-throughput assignment of MMAB to the mitochondrion from a quantitative high-confidence
      human mitochondrial proteome. Consistent with the transit peptide and matrix function.
    action: ACCEPT
    reason: >-
      Correct compartment, corroborating the UniProt localization and the enzyme's matrix role.
    supported_by:
    - reference_id: PMID:33797888
      supporting_text: >-
        In the matrix, adenosyltransferase (ATR, also known as MMAB or CblB) and CblA (or MMAA),
        a G-protein chaperone, are recruited for the synthesis and delivery of AdoCbl to the
        target enzyme, MCM (or Mut)
- term:
    id: GO:0009235
    label: cobalamin metabolic process
  evidence_type: IDA
  original_reference_id: PMID:12514191
  qualifier: involved_in
  review:
    summary: >-
      Direct experimental evidence placing MMAB in cobalamin metabolism: the human ATR cDNA
      complemented an ATR-deficient bacterial mutant and its dysregulation was shown in cblB
      methylmalonic aciduria cell lines, establishing MMAB as the enzyme performing the terminal
      conversion of cobalamin to coenzyme B12.
    action: ACCEPT
    reason: >-
      Well-supported biological-process annotation from the defining functional study of MMAB.
    supported_by:
    - reference_id: PMID:12514191
      supporting_text: >-
        We propose that inborn errors in the human ATR gene identified here result in methylmalonyl
        aciduria.
- term:
    id: GO:0016765
    label: transferase activity, transferring alkyl or aryl (other than methyl) groups
  evidence_type: IDA
  original_reference_id: PMID:12514191
  qualifier: enables
  review:
    summary: >-
      Direct evidence that MMAB is a transferase transferring a (non-methyl) alkyl group — the
      5'-deoxyadenosyl group — but this is a parent term of the specific corrinoid adenosyltransferase
      activity (GO:0008817 is a subclass of GO:0016765). The specific term is warranted.
    action: MODIFY
    reason: >-
      Correct in essence but too general: the transferred group is specifically the deoxyadenosyl
      moiety onto cob(I)alamin, which is captured precisely by GO:0008817 corrinoid adenosyltransferase
      activity (an is-a descendant of GO:0016765). Replace with the specific term.
    proposed_replacement_terms:
    - id: GO:0008817
      label: corrinoid adenosyltransferase activity
    supported_by:
    - reference_id: PMID:12514191
      supporting_text: >-
        ATP:cob(I)alamin adenosyltransferase (ATR) catalyzes the terminal step in the conversion
        of cobalamins into Ado-B12.
- term:
    id: GO:0009235
    label: cobalamin metabolic process
  evidence_type: TAS
  original_reference_id: PMID:28497574
  qualifier: involved_in
  review:
    summary: >-
      Traceable author statement placing MMAB in cobalamin metabolism: the paper describes MMAB as the
      adenosyltransferase that generates AdoCbl for delivery to methylmalonyl-CoA mutase.
    action: ACCEPT
    reason: >-
      Correct biological process; the source explicitly frames MMAB as the AdoCbl-generating enzyme
      in the mitochondrial cobalamin pathway.
    supported_by:
    - reference_id: PMID:28497574
      supporting_text: >-
        MMAA regulates the incorporation of the cofactor adenosylcobalamin (AdoCbl), generated from
        the MMAB adenosyltransferase, into the destination enzyme methylmalonyl-CoA mutase (MUT).
- term:
    id: GO:0031419
    label: cobalamin binding
  evidence_type: IDA
  original_reference_id: PMID:28497574
  qualifier: enables
  review:
    summary: >-
      Direct evidence that MMAB binds cobalamin (adenosylcobalamin). MMAB binds the cofactor in a
      base-off state and holds the AdoCbl product prior to hand-off to the mutase; UniProt cites this
      reference for adenosylcobalamin-binding.
    action: ACCEPT
    reason: >-
      Cobalamin binding is an integral, experimentally supported feature of MMAB's function as a B12
      adenosyltransferase and escort.
    supported_by:
    - reference_id: PMID:28497574
      supporting_text: >-
        MMAA regulates the incorporation of the cofactor adenosylcobalamin (AdoCbl), generated from
        the MMAB adenosyltransferase, into the destination enzyme methylmalonyl-CoA mutase (MUT).
- term:
    id: GO:0008817
    label: corrinoid adenosyltransferase activity
  evidence_type: IDA
  original_reference_id: PMID:12514191
  qualifier: enables
  review:
    summary: >-
      Direct experimental demonstration of corrinoid (cob(I)alamin) adenosyltransferase activity for
      the human enzyme: recombinant human ATR produced measurable ATR activity and complemented an
      ATR-deficient bacterial mutant for Ado-B12-dependent growth.
    action: ACCEPT
    reason: >-
      Gold-standard direct assay of the core molecular function on the human protein.
    supported_by:
    - reference_id: PMID:12514191
      supporting_text: >-
        Enzyme assays showed that expression strains produced 87 and 98 nmol/min/mg ATR activity,
        respectively.
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-3322125
  qualifier: located_in
  review:
    summary: >-
      Reactome-curated mitochondrial matrix localization for MMAB, the compartment where AdoCbl is
      synthesized and delivered to methylmalonyl-CoA mutase.
    action: ACCEPT
    reason: >-
      Correct and appropriately specific subcellular location, consistent with the matrix role of the
      AdoCbl-synthesis/delivery machinery.
    supported_by:
    - reference_id: PMID:33797888
      supporting_text: >-
        In the matrix, adenosyltransferase (ATR, also known as MMAB or CblB) and CblA (or MMAA),
        a G-protein chaperone, are recruited for the synthesis and delivery of AdoCbl to the
        target enzyme, MCM (or Mut)
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-3159253
  qualifier: located_in
  review:
    summary: >-
      Reactome-curated mitochondrial matrix localization (from the MMAB adenosylates cob(I)alamin
      reaction). Duplicate compartment assignment; correct.
    action: ACCEPT
    reason: >-
      Correct specific location; consistent with the enzyme's matrix function.
    supported_by:
    - reference_id: PMID:33797888
      supporting_text: >-
        In the matrix, adenosyltransferase (ATR, also known as MMAB or CblB) and CblA (or MMAA),
        a G-protein chaperone, are recruited for the synthesis and delivery of AdoCbl to the
        target enzyme, MCM (or Mut)
- term:
    id: GO:0005524
    label: ATP binding
  evidence_type: IDA
  original_reference_id: PMID:17176040
  qualifier: enables
  review:
    summary: >-
      ATP binding is a defining feature of MMAB: it is the adenosyl-donor cosubstrate and ATP binding
      also organizes the high-affinity cobalamin pocket and gates cofactor delivery to the mutase.
      The ATP-bound human ATR crystal structure (PDB 2IDX) and UniProt ATP-binding features
      (residues 60-63, 68-69, 78, 190-194, 214) directly establish this. Present in UniProt (GO:0005524
      IEA:UniProtKB-KW) but absent from the current GOA TSV, so added here.
    action: NEW
    reason: >-
      Structurally and biochemically established, functionally central molecular function (ATP is the
      adenosyl donor) that is missing from the GOA set; added with the ATP-bound structure as evidence.
    supported_by:
    - reference_id: PMID:33797888
      supporting_text: >-
        ATP binding organizes a high affinity cob(II)alamin pocket in human ATR.
core_functions:
- description: >-
    Catalyses the terminal step of adenosylcobalamin (coenzyme B12) synthesis, transferring the
    5'-deoxyadenosyl group from ATP to reduced cob(I)alamin to produce adenosylcob(III)alamin, and
    uses ATP as the adenosyl donor.
  molecular_function:
    id: GO:0008817
    label: corrinoid adenosyltransferase activity
  supported_by:
  - reference_id: PMID:12514191
    supporting_text: >-
      ATP:cob(I)alamin adenosyltransferase (ATR) catalyzes the terminal step in the conversion
      of cobalamins into Ado-B12.
  - reference_id: PMID:30282455
    supporting_text: >-
      AdoCbl is synthesized by adenosyltransferase (ATR), which catalyzes the adenosylation of
      cob(I)alamin by ATP in a direct nucleophilic displacement reaction that leads to
      cobalt−carbon (Co−C) bond formation yielding AdoCbl and inorganic triphosphate
  directly_involved_in:
  - id: GO:0009235
    label: cobalamin metabolic process
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
- description: >-
    Binds cobalamin (in a base-off state) and, in an ATP-dependent manner, holds the AdoCbl product
    and delivers it directly to methylmalonyl-CoA mutase, functioning as a cobalamin-binding cofactor
    escort in the mitochondrial matrix.
  molecular_function:
    id: GO:0031419
    label: cobalamin binding
  supported_by:
  - reference_id: PMID:30282455
    supporting_text: >-
      ATR also delivers the AdoCbl product directly to MCM, thereby averting cofactor loss by
      release into solution.
  - reference_id: PMID:28497574
    supporting_text: >-
      MMAA regulates the incorporation of the cofactor adenosylcobalamin (AdoCbl), generated from
      the MMAB adenosyltransferase, into the destination enzyme methylmalonyl-CoA mutase (MUT).
  directly_involved_in:
  - id: GO:0009235
    label: cobalamin metabolic process
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
references:
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: PMID:12514191
  title: Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase
    cDNAs based on complementation of a bacterial mutant.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Defining functional study of human MMAB/ATR; directly establishes corrinoid adenosyltransferase
      activity, the AdoCbl-synthesis role, and the link to cblB methylmalonic aciduria. Abstract-only
      in cache but supporting quotes verified verbatim against the cached record.
- id: PMID:15913339
  title: Spectroscopic evidence for the formation of a four-coordinate Co2+ cobalamin
    species upon binding to the human ATP:cobalamin adenosyltransferase.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Spectroscopy of the human ATR mechanism (cobalamin binding, ATP-dependent coordination
      chemistry); supports the adenosyltransferase activity and cobalamin binding.
- id: PMID:25910212
  title: Widespread macromolecular interaction perturbations in human genetic disorders.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Large-scale interactome perturbation study; source of a generic protein-binding IPI (CBY2). Does
      not characterize MMAB function.
- id: PMID:28497574
  title: Protein destabilization and loss of protein-protein interaction are fundamental
    mechanisms in cblA-type methylmalonic aciduria.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Primarily an MMAA (cblA) study, but assays MMAB adenosylcobalamin binding and the MMAB->MUT
      AdoCbl transfer; UniProt cites it for MMAB adenosylcobalamin-binding. Abstract-only in cache;
      supporting quotes verified verbatim.
- id: PMID:30282455
  title: Sacrificial Cobalt-Carbon Bond Homolysis in Coenzyme B(12) as a Cofactor
    Conservation Strategy.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Full text available; directly documents MMAB/ATR AdoCbl synthesis, direct delivery to MCM, and
      the sacrificial Co-C homolysis cofactor-conservation activity.
- id: PMID:32814053
  title: Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins
    and Uncovers Widespread Protein Aggregation in Affected Brains.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Large-scale neurodegenerative-disease interactome; source of generic protein-binding IPIs
      (CALR, DLST, NEK7, OPTN). No functional MMAB characterization.
- id: PMID:33797888
  title: Redox-Linked Coordination Chemistry Directs Vitamin B(12) Trafficking.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Authoritative account of the mitochondrial B12 trafficking pathway; describes MMAB/ATR as the
      homotrimeric adenosyltransferase and escort in the matrix. Full text available; quotes verified.
- id: PMID:33961781
  title: Dual proteome-scale networks reveal cell-specific remodeling of the human
    interactome.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Proteome-scale interactome; source of a generic protein-binding IPI (DBT). No functional MMAB
      characterization.
- id: PMID:34800366
  title: Quantitative high-confidence human mitochondrial proteome and its dynamics
    in cellular context.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      High-confidence mitochondrial proteome supporting MMAB mitochondrial localization (HTP).
- id: PMID:40205054
  title: Multimodal cell maps as a foundation for structural and functional genomics.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Multimodal cell-map resource; source of a generic protein-binding IPI (DBT). No functional MMAB
      characterization.
- id: PMID:17176040
  title: Structure of ATP-bound human ATP:cobalamin adenosyltransferase.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Crystal structure of ATP-bound human MMAB (PDB 2IDX), establishing the homotrimer and ATP
      binding site; cited by UniProt for ATP-binding features and SUBUNIT. Used to support the NEW
      ATP binding annotation.
- id: Reactome:R-HSA-3159253
  title: MMAB adenosylates cob(I)alamin
  findings: []
- id: Reactome:R-HSA-3322125
  title: Defective MMAB does not transfer adenosyl group from ATP to B12s
  findings: []
- id: Reactome:R-HSA-9759218
  title: Cobalamin (Cbl) metabolism
  findings: []