Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9D273 (MMAB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·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 homolog
Gene names
Name:Mmab
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the Cob(I)alamin adenosyltransferase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcobalamin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functionATP 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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D273-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9D273-2)

The sequence of this isoform differs from the canonical sequence as follows:
     210-237: LSDYLFTVARYAAMKEGSQEKIYKKHDV → CLSGVWRVCL...LGNKSQRRHT
Note: Due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 237211Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
PRO_0000005569

Regions

Nucleotide binding54 – 574ATP By similarity
Nucleotide binding62 – 632ATP By similarity
Nucleotide binding184 – 1885ATP By similarity

Sites

Binding site721ATP By similarity
Binding site2081ATP By similarity

Natural variations

Alternative sequence210 – 23728LSDYL…KKHDV → CLSGVWRVCLTTRPLPSSCI LDCAVSPVALSHSEVRLCLG NKSQRRHT in isoform 2.
VSP_008847

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: CB0408BC575FE8CB

FASTA23726,273
        10         20         30         40         50         60 
MAVWLFGGRL GLRGRLSACR LLCPRFQSRG PQGGEDGDRL QPSSTAAKIP KIYTKTGDKG 

        70         80         90        100        110        120 
FSSTFTGERR PKDDQVFEAV GTTDELSSAI GFAMELVTEK GHMFAEELQK IQCMLQDVGS 

       130        140        150        160        170        180 
ALATPRSSAR EAHLKHTAFQ EGPVLELERW IDKYSSQLPP LKAFILPSGG KSSSALHFCR 

       190        200        210        220        230 
AVCRRAERRV VPLVQMGETD ANVAKFLNRL SDYLFTVARY AAMKEGSQEK IYKKHDV

« Hide

Isoform 2 [UniParc].

Checksum: 32F55E6662F598C4
Show »

FASTA25728,233

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
Tissue: Cecum, Diencephalon and Thymus.
[2]"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] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain and Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK020286 mRNA. Translation: BAB32055.1.
AK034288 mRNA. Translation: BAC28659.1.
AK088785 mRNA. Translation: BAC40571.1.
AK148421 mRNA. Translation: BAE28544.1.
BC022159 mRNA. Translation: AAH22159.1.
BC057558 mRNA. Translation: AAH57558.1.
IPIIPI00228497.
IPI00283203.
RefSeqNP_084232.1. NM_029956.3.
UniGeneMm.105182.

3D structure databases

ProteinModelPortalQ9D273.
SMRQ9D273. Positions 52-234.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000098418.

PTM databases

PhosphoSiteQ9D273.

Proteomic databases

PaxDbQ9D273.
PRIDEQ9D273.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031560; ENSMUSP00000031560; ENSMUSG00000029575.
GeneID77697.
KEGGmmu:77697.
UCSCuc008yzo.1. mouse.
uc008yzp.1. mouse.

Organism-specific databases

CTD326625.
MGIMGI:1924947. Mmab.

Phylogenomic databases

eggNOGCOG2096.
GeneTreeENSGT00390000008432.
HOGENOMHOG000291639.
HOVERGENHBG045589.
KOK00798.
OMAVLWVPGK.
OrthoDBEOG4C5CKM.

Enzyme and pathway databases

UniPathwayUPA00148; UER00233.

Gene expression databases

ArrayExpressQ9D273.
BgeeQ9D273.
GenevestigatorQ9D273.
GermOnlineENSMUSG00000029575. Mus musculus.

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. AdoCbl_synth_CblAdoTrfase-like. 1 hit.
TIGRFAMsTIGR00636. PduO_Nterm. 1 hit.
ProtoNetSearch...

Other

NextBio347375.
SOURCESearch...

Entry information

Entry nameMMAB_MOUSE
AccessionPrimary (citable) accession number: Q9D273
Secondary accession number(s): Q3UFL6, Q8CBZ0, Q8VBZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents