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

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Q96EY8 (MMAB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (7) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

MMAB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cobalamin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cob(I)yrinic acid a,c-diamide adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 32

Mitochondrion Potential

Chain

33 – 250

218

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

PRO_0000005568

Regions

Nucleotide binding

60 – 63

ATP

Nucleotide binding

68 – 69

ATP

Nucleotide binding

190 – 194

ATP

Sites

Binding site

ATP

Binding site

214

ATP

Natural variations

Natural variant

R → H.
Corresponds to variant rs10774775 [ dbSNP | Ensembl ].

VAR_038803

Natural variant

R → Q. Ref.1 Ref.2 Ref.4
Corresponds to variant rs36013132 [ dbSNP | Ensembl ].

VAR_017203

Natural variant

I → T in MMAB. Ref.7

VAR_023471

Natural variant

135

A → T in MMAB. Ref.1
Corresponds to variant rs35648932 [ dbSNP | Ensembl ].

VAR_017204

Natural variant

186

R → W. Ref.1
Corresponds to variant rs28941784 [ dbSNP | Ensembl ].

VAR_017205

Natural variant

191

R → W in MMAB. Ref.1 Ref.7

VAR_017206

Natural variant

193

E → K in MMAB. Ref.1

VAR_017207

Natural variant

239

M → 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

Length

Mass (Da)

Tools

Q96EY8 [UniParc].

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

FASTA

250

27,388

        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' referencesShow '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

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF550404

AF550403 Genomic DNA. Translation: AAN85091.1.
FJ515859 Genomic DNA. Translation: ACS13749.1.
BC005054 mRNA. Translation: AAH05054.2.
BC011831 mRNA. Translation: AAH11831.1.

IPI

IPI00029665.

RefSeq

NP_443077.1. NM_052845.3.

UniGene

Hs.12106.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IDX	X-ray	2.50	A/B/C	56-250	[»]

ProteinModelPortal

Q96EY8.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000266839.

PTM databases

PhosphoSite

Q96EY8.

Polymorphism databases

DMDM

38258221.

Proteomic databases

PaxDb

Q96EY8.

PeptideAtlas

Q96EY8.

PRIDE

Q96EY8.

Protocols and materials databases

DNASU

326625.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000545712; ENSP00000445920; ENSG00000139428.

GeneID

326625.

KEGG

hsa:326625.

UCSC

uc001tou.3. human.

Organism-specific databases

CTD

326625.

GeneCards

GC12M109991.

HGNC

HGNC:19331. MMAB.

HPA

HPA039017.

MIM

251110. phenotype.
607568. gene.

neXtProt

NX_Q96EY8.

Orphanet

79311. Vitamin B12-responsive methylmalonic acidemia type cblB.

PharmGKB

PA134864025.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2096.

HOGENOM

HOG000291639.

HOVERGEN

HBG045589.

InParanoid

Q96EY8.

K00798.

OMA

VLWVPGK.

OrthoDB

EOG4C5CKM.

PhylomeDB

Q96EY8.

Enzyme and pathway databases

UniPathway

UPA00148; UER00233.

Gene expression databases

ArrayExpress

Q96EY8.

Bgee

Q96EY8.

CleanEx

HS_MMAB.

Genevestigator

Q96EY8.

GermOnline

ENSG00000139428. Homo sapiens.

Family and domain databases

Gene3D

1.20.1200.10. 1 hit.

InterPro

IPR016030. AdoCbl_synth_CblAdoTrfase-like.
[Graphical view]

Pfam

PF01923. Cob_adeno_trans. 1 hit.
[Graphical view]

ProDom

PD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF89028. AdoCbl_synth_CblAdoTrfase-like. 1 hit.

TIGRFAMs

TIGR00636. PduO_Nterm. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

EvolutionaryTrace

Q96EY8.

GenomeRNAi

326625.

NextBio

96712.

SOURCE

Search...

Entry information

Entry name

MMAB_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.