Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial

Gene

MMAB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + cob(I)yrinic acid a,c-diamide = triphosphate + adenosylcob(III)yrinic acid a,c-diamide.
ATP + cobinamide = triphosphate + adenosylcobinamide.

Pathwayi: adenosylcobalamin biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes adenosylcobalamin from cob(II)yrinate a,c-diamide.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial (MMAB)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
  7. no protein annotated in this organism
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes adenosylcobalamin from cob(II)yrinate a,c-diamide, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei78ATP1 Publication1
Binding sitei214ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi60 – 63ATP1 Publication4
Nucleotide bindingi68 – 69ATP1 Publication2
Nucleotide bindingi190 – 194ATP1 Publication5

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cob(I)yrinic acid a,c-diamide adenosyltransferase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS13779-MONOMER.
BRENDAi2.5.1.17. 2681.
ReactomeiR-HSA-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
UniPathwayiUPA00148; UER00233.

Names & Taxonomyi

Protein namesi
Recommended name:
Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial (EC:2.5.1.17)
Alternative name(s):
Cob(I)alamin adenosyltransferase
Methylmalonic aciduria type B protein
Gene namesi
Name:MMAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:19331. MMAB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Methylmalonic aciduria type cblB (MMAB)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of methylmalonate and cobalamin metabolism due to defective synthesis of adenosylcobalamin.
See also OMIM:251110
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02347196I → T in MMAB. 1 Publication1
Natural variantiVAR_017204135A → T in MMAB. 1 PublicationCorresponds to variant rs35648932dbSNPEnsembl.1
Natural variantiVAR_017206191R → W in MMAB. 2 PublicationsCorresponds to variant rs376128990dbSNPEnsembl.1
Natural variantiVAR_017207193E → K in MMAB. 1 PublicationCorresponds to variant rs749758687dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi326625.
MalaCardsiMMAB.
MIMi251110. phenotype.
OpenTargetsiENSG00000139428.
Orphaneti79311. Vitamin B12-responsive methylmalonic acidemia type cblB.
PharmGKBiPA134864025.

Chemistry databases

DrugBankiDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

Polymorphism and mutation databases

BioMutaiMMAB.
DMDMi38258221.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 32MitochondrionSequence analysisAdd BLAST32
ChainiPRO_000000556833 – 250Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrialAdd BLAST218

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei134PhosphoserineCombined sources1
Modified residuei211N6-succinyllysineBy similarity1
Modified residuei230N6-acetyllysine; alternateBy similarity1
Modified residuei230N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96EY8.
MaxQBiQ96EY8.
PaxDbiQ96EY8.
PeptideAtlasiQ96EY8.
PRIDEiQ96EY8.

PTM databases

iPTMnetiQ96EY8.
PhosphoSitePlusiQ96EY8.

Expressioni

Tissue specificityi

Expressed in liver and skeletal muscle.

Gene expression databases

BgeeiENSG00000139428.
CleanExiHS_MMAB.
ExpressionAtlasiQ96EY8. baseline and differential.
GenevisibleiQ96EY8. HS.

Organism-specific databases

HPAiHPA039017.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi130605. 15 interactors.
IntActiQ96EY8. 1 interactor.
STRINGi9606.ENSP00000445920.

Structurei

Secondary structure

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni62 – 65Combined sources4
Beta strandi66 – 69Combined sources4
Beta strandi75 – 77Combined sources3
Helixi80 – 100Combined sources21
Helixi109 – 128Combined sources20
Helixi137 – 139Combined sources3
Helixi148 – 162Combined sources15
Helixi177 – 196Combined sources20
Turni197 – 203Combined sources7
Helixi207 – 231Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IDXX-ray2.50A/B/C56-250[»]
ProteinModelPortaliQ96EY8.
SMRiQ96EY8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96EY8.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IEUE. Eukaryota.
COG2096. LUCA.
GeneTreeiENSGT00390000008432.
HOGENOMiHOG000291639.
HOVERGENiHBG045589.
InParanoidiQ96EY8.
KOiK00798.
OMAiGADLCTP.
OrthoDBiEOG091G0JU1.
PhylomeDBiQ96EY8.
TreeFamiTF312942.

Family and domain databases

Gene3Di1.20.1200.10. 1 hit.
InterProiIPR016030. AdoCbl_synth_CblAdoTrfase-like.
IPR029499. PduO-typ.
[Graphical view]
PfamiPF01923. Cob_adeno_trans. 1 hit.
[Graphical view]
ProDomiPD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF89028. SSF89028. 1 hit.
TIGRFAMsiTIGR00636. PduO_Nterm. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96EY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVCGLGSRL GLGSRLGLRG CFGAARLLYP RFQSRGPQGV EDGDRPQPSS
60 70 80 90 100
KTPRIPKIYT KTGDKGFSST FTGERRPKDD QVFEAVGTTD ELSSAIGFAL
110 120 130 140 150
ELVTEKGHTF AEELQKIQCT LQDVGSALAT PCSSAREAHL KYTTFKAGPI
160 170 180 190 200
LELEQWIDKY TSQLPPLTAF ILPSGGKISS ALHFCRAVCR RAERRVVPLV
210 220 230 240 250
QMGETDANVA KFLNRLSDYL FTLARYAAMK EGNQEKIYMK NDPSAESEGL
Length:250
Mass (Da):27,388
Last modified:December 1, 2001 - v1
Checksum:iAEFC4E487C9FA5AB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03880319R → H.Corresponds to variant rs10774775dbSNPEnsembl.1
Natural variantiVAR_01720319R → Q.3 PublicationsCorresponds to variant rs36013132dbSNPEnsembl.1
Natural variantiVAR_02347196I → T in MMAB. 1 Publication1
Natural variantiVAR_017204135A → T in MMAB. 1 PublicationCorresponds to variant rs35648932dbSNPEnsembl.1
Natural variantiVAR_017205186R → W.1 PublicationCorresponds to variant rs28941784dbSNPEnsembl.1
Natural variantiVAR_017206191R → W in MMAB. 2 PublicationsCorresponds to variant rs376128990dbSNPEnsembl.1
Natural variantiVAR_017207193E → K in MMAB. 1 PublicationCorresponds to variant rs749758687dbSNPEnsembl.1
Natural variantiVAR_017208239M → K Common polymorphism. 3 PublicationsCorresponds to variant rs9593dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF550404
, AF550396, AF550397, AF550398, AF550399, AF550400, AF550401, AF550402, AF550403 Genomic DNA. Translation: AAN85091.1.
FJ515859 Genomic DNA. Translation: ACS13749.1.
BC005054 mRNA. Translation: AAH05054.2.
BC011831 mRNA. Translation: AAH11831.1.
CCDSiCCDS9131.1.
RefSeqiNP_443077.1. NM_052845.3.
UniGeneiHs.12106.

Genome annotation databases

EnsembliENST00000545712; ENSP00000445920; ENSG00000139428.
GeneIDi326625.
KEGGihsa:326625.
UCSCiuc001tou.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF550404
, AF550396, AF550397, AF550398, AF550399, AF550400, AF550401, AF550402, AF550403 Genomic DNA. Translation: AAN85091.1.
FJ515859 Genomic DNA. Translation: ACS13749.1.
BC005054 mRNA. Translation: AAH05054.2.
BC011831 mRNA. Translation: AAH11831.1.
CCDSiCCDS9131.1.
RefSeqiNP_443077.1. NM_052845.3.
UniGeneiHs.12106.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IDXX-ray2.50A/B/C56-250[»]
ProteinModelPortaliQ96EY8.
SMRiQ96EY8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130605. 15 interactors.
IntActiQ96EY8. 1 interactor.
STRINGi9606.ENSP00000445920.

Chemistry databases

DrugBankiDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

PTM databases

iPTMnetiQ96EY8.
PhosphoSitePlusiQ96EY8.

Polymorphism and mutation databases

BioMutaiMMAB.
DMDMi38258221.

Proteomic databases

EPDiQ96EY8.
MaxQBiQ96EY8.
PaxDbiQ96EY8.
PeptideAtlasiQ96EY8.
PRIDEiQ96EY8.

Protocols and materials databases

DNASUi326625.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000545712; ENSP00000445920; ENSG00000139428.
GeneIDi326625.
KEGGihsa:326625.
UCSCiuc001tou.4. human.

Organism-specific databases

CTDi326625.
DisGeNETi326625.
GeneCardsiMMAB.
GeneReviewsiMMAB.
HGNCiHGNC:19331. MMAB.
HPAiHPA039017.
MalaCardsiMMAB.
MIMi251110. phenotype.
607568. gene.
neXtProtiNX_Q96EY8.
OpenTargetsiENSG00000139428.
Orphaneti79311. Vitamin B12-responsive methylmalonic acidemia type cblB.
PharmGKBiPA134864025.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEUE. Eukaryota.
COG2096. LUCA.
GeneTreeiENSGT00390000008432.
HOGENOMiHOG000291639.
HOVERGENiHBG045589.
InParanoidiQ96EY8.
KOiK00798.
OMAiGADLCTP.
OrthoDBiEOG091G0JU1.
PhylomeDBiQ96EY8.
TreeFamiTF312942.

Enzyme and pathway databases

UniPathwayiUPA00148; UER00233.
BioCyciZFISH:HS13779-MONOMER.
BRENDAi2.5.1.17. 2681.
ReactomeiR-HSA-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.

Miscellaneous databases

EvolutionaryTraceiQ96EY8.
GeneWikiiMMAB.
GenomeRNAii326625.
PROiQ96EY8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000139428.
CleanExiHS_MMAB.
ExpressionAtlasiQ96EY8. baseline and differential.
GenevisibleiQ96EY8. HS.

Family and domain databases

Gene3Di1.20.1200.10. 1 hit.
InterProiIPR016030. AdoCbl_synth_CblAdoTrfase-like.
IPR029499. PduO-typ.
[Graphical view]
PfamiPF01923. Cob_adeno_trans. 1 hit.
[Graphical view]
ProDomiPD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF89028. SSF89028. 1 hit.
TIGRFAMsiTIGR00636. PduO_Nterm. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMMAB_HUMAN
AccessioniPrimary (citable) accession number: Q96EY8
Secondary accession number(s): C5HU05, Q9BSH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.