Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96EY8 (MMAB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MMAB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

ATP + cobinamide = triphosphate + adenosylcobinamide.

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.

Subunit structure

Homotrimer. Ref.6

Subcellular location

Mitochondrion Probable.

Tissue specificity

Expressed in liver and skeletal muscle.

Involvement in disease

Methylmalonic aciduria type cblB (MMAB) [MIM:251110]: A disorder of methylmalonate and cobalamin metabolism due to defective synthesis of adenosylcobalamin.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.7

Sequence similarities

Belongs to the Cob(I)alamin adenosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion Potential
Chain33 – 250218Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
PRO_0000005568

Regions

Nucleotide binding60 – 634ATP
Nucleotide binding68 – 692ATP
Nucleotide binding190 – 1945ATP

Sites

Binding site781ATP
Binding site2141ATP

Amino acid modifications

Modified residue2111N6-succinyllysine By similarity
Modified residue2301N6-acetyllysine; alternate By similarity
Modified residue2301N6-succinyllysine; alternate By similarity

Natural variations

Natural variant191R → H.
Corresponds to variant rs10774775 [ dbSNP | Ensembl ].
VAR_038803
Natural variant191R → Q. Ref.1 Ref.2 Ref.4
Corresponds to variant rs36013132 [ dbSNP | Ensembl ].
VAR_017203
Natural variant961I → T in MMAB. Ref.7
VAR_023471
Natural variant1351A → T in MMAB. Ref.1
Corresponds to variant rs35648932 [ dbSNP | Ensembl ].
VAR_017204
Natural variant1861R → W. Ref.1
Corresponds to variant rs28941784 [ dbSNP | Ensembl ].
VAR_017205
Natural variant1911R → W in MMAB. Ref.1 Ref.7
VAR_017206
Natural variant1931E → K in MMAB. Ref.1
VAR_017207
Natural variant2391M → K Common polymorphism. Ref.1 Ref.2 Ref.4
Corresponds to variant rs9593 [ dbSNP | Ensembl ].
VAR_017208

Secondary structure

............ 250
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96EY8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: AEFC4E487C9FA5AB

FASTA25027,388
        10         20         30         40         50         60 
MAVCGLGSRL GLGSRLGLRG CFGAARLLYP RFQSRGPQGV EDGDRPQPSS KTPRIPKIYT 

        70         80         90        100        110        120 
KTGDKGFSST FTGERRPKDD QVFEAVGTTD ELSSAIGFAL ELVTEKGHTF AEELQKIQCT 

       130        140        150        160        170        180 
LQDVGSALAT PCSSAREAHL KYTTFKAGPI LELEQWIDKY TSQLPPLTAF ILPSGGKISS 

       190        200        210        220        230        240 
ALHFCRAVCR RAERRVVPLV QMGETDANVA KFLNRLSDYL FTLARYAAMK EGNQEKIYMK 

       250 
NDPSAESEGL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the gene responsible for the cblB complementation group of vitamin B(12)-dependent methylmalonic aciduria."
Dobson C.M., Wai T., Leclerc D., Kadir H., Narang M., Lerner-Ellis J.P., Hudson T.J., Rosenblatt D.S., Gravel R.A.
Hum. Mol. Genet. 11:3361-3369(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MMAB THR-135; TRP-191 AND LYS-193, VARIANTS GLN-19; TRP-186 AND LYS-239.
[2]"Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant."
Leal N.A., Park S.D., Kima P.E., Bobik T.A.
J. Biol. Chem. 278:9227-9234(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLN-19 AND LYS-239, INVOLVEMENT IN DISEASE.
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLN-19 AND LYS-239.
Tissue: Lung.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Structure of ATP-bound human ATP:cobalamin adenosyltransferase."
Schubert H.L., Hill C.P.
Biochemistry 45:15188-15196(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 55-250 IN COMPLEX WITH ATP, SUBUNIT.
[7]"Genetic analysis of three genes causing isolated methylmalonic acidemia: identification of 21 novel allelic variants."
Martinez M.A., Rincon A., Desviat L.R., Merinero B., Ugarte M., Perez B.
Mol. Genet. Metab. 84:317-325(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAB THR-96 AND TRP-191.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF550404 expand/collapse EMBL AC list , 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.
RefSeqNP_443077.1. NM_052845.3.
UniGeneHs.12106.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IDXX-ray2.50A/B/C56-250[»]
ProteinModelPortalQ96EY8.
SMRQ96EY8. Positions 58-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130605. 1 interaction.
IntActQ96EY8. 1 interaction.
STRING9606.ENSP00000266839.

Chemistry

DrugBankDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

PTM databases

PhosphoSiteQ96EY8.

Polymorphism databases

DMDM38258221.

Proteomic databases

PaxDbQ96EY8.
PeptideAtlasQ96EY8.
PRIDEQ96EY8.

Protocols and materials databases

DNASU326625.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000545712; ENSP00000445920; ENSG00000139428.
GeneID326625.
KEGGhsa:326625.
UCSCuc001tou.3. human.

Organism-specific databases

CTD326625.
GeneCardsGC12M109991.
HGNCHGNC:19331. MMAB.
HPAHPA039017.
MIM251110. phenotype.
607568. gene.
neXtProtNX_Q96EY8.
Orphanet79311. Vitamin B12-responsive methylmalonic acidemia type cblB.
PharmGKBPA134864025.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2096.
HOGENOMHOG000291639.
HOVERGENHBG045589.
InParanoidQ96EY8.
KOK00798.
OMAVLWVPGK.
OrthoDBEOG7X3QS4.
PhylomeDBQ96EY8.
TreeFamTF312942.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00148; UER00233.

Gene expression databases

ArrayExpressQ96EY8.
BgeeQ96EY8.
CleanExHS_MMAB.
GenevestigatorQ96EY8.

Family and domain databases

Gene3D1.20.1200.10. 1 hit.
InterProIPR016030. AdoCbl_synth_CblAdoTrfase-like.
[Graphical view]
PfamPF01923. Cob_adeno_trans. 1 hit.
[Graphical view]
ProDomPD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF89028. SSF89028. 1 hit.
TIGRFAMsTIGR00636. PduO_Nterm. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ96EY8.
GeneWikiMMAB.
GenomeRNAi326625.
NextBio96712.
PROQ96EY8.
SOURCESearch...

Entry information

Entry nameMMAB_HUMAN
AccessionPrimary (citable) accession number: Q96EY8
Secondary accession number(s): C5HU05, Q9BSH0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM