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Q9D273

- MMAB_MOUSE

UniProt

Q9D273 - MMAB_MOUSE

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Protein
Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
Gene
Mmab
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721ATP By similarity
Binding sitei208 – 2081ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi54 – 574ATP By similarity
Nucleotide bindingi62 – 632ATP By similarity
Nucleotide bindingi184 – 1885ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cob(I)yrinic acid a,c-diamide adenosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cobalamin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_189118. 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 homolog
Gene namesi
Name:Mmab
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1924947. Mmab.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626Mitochondrion Reviewed prediction
Add
BLAST
Chaini27 – 237211Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
PRO_0000005569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051N6-succinyllysine1 Publication
Modified residuei224 – 2241N6-acetyllysine; alternate1 Publication
Modified residuei224 – 2241N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D273.
PaxDbiQ9D273.
PRIDEiQ9D273.

PTM databases

PhosphoSiteiQ9D273.

Expressioni

Gene expression databases

ArrayExpressiQ9D273.
BgeeiQ9D273.
GenevestigatoriQ9D273.

Interactioni

Subunit structurei

Homotrimer By similarity.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000098418.

Structurei

3D structure databases

ProteinModelPortaliQ9D273.
SMRiQ9D273. Positions 52-234.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2096.
GeneTreeiENSGT00390000008432.
HOGENOMiHOG000291639.
HOVERGENiHBG045589.
KOiK00798.
OMAiFVAARHA.
OrthoDBiEOG7X3QS4.
PhylomeDBiQ9D273.
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.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9D273-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAVWLFGGRL GLRGRLSACR LLCPRFQSRG PQGGEDGDRL QPSSTAAKIP    50
KIYTKTGDKG FSSTFTGERR PKDDQVFEAV GTTDELSSAI GFAMELVTEK 100
GHMFAEELQK IQCMLQDVGS ALATPRSSAR EAHLKHTAFQ EGPVLELERW 150
IDKYSSQLPP LKAFILPSGG KSSSALHFCR AVCRRAERRV VPLVQMGETD 200
ANVAKFLNRL SDYLFTVARY AAMKEGSQEK IYKKHDV 237
Length:237
Mass (Da):26,273
Last modified:June 1, 2001 - v1
Checksum:iCB0408BC575FE8CB
GO
Isoform 2 (identifier: Q9D273-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:257
Mass (Da):28,233
Checksum:i32F55E6662F598C4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei210 – 23728LSDYL…KKHDV → CLSGVWRVCLTTRPLPSSCI LDCAVSPVALSHSEVRLCLG NKSQRRHT in isoform 2.
VSP_008847Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS19565.1. [Q9D273-1]
RefSeqiNP_084232.1. NM_029956.3. [Q9D273-1]
XP_006530568.1. XM_006530505.1. [Q9D273-2]
UniGeneiMm.105182.

Genome annotation databases

EnsembliENSMUST00000031560; ENSMUSP00000031560; ENSMUSG00000029575. [Q9D273-1]
GeneIDi77697.
KEGGimmu:77697.
UCSCiuc008yzo.1. mouse. [Q9D273-1]
uc008yzp.1. mouse. [Q9D273-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS19565.1. [Q9D273-1 ]
RefSeqi NP_084232.1. NM_029956.3. [Q9D273-1 ]
XP_006530568.1. XM_006530505.1. [Q9D273-2 ]
UniGenei Mm.105182.

3D structure databases

ProteinModelPortali Q9D273.
SMRi Q9D273. Positions 52-234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000098418.

PTM databases

PhosphoSitei Q9D273.

Proteomic databases

MaxQBi Q9D273.
PaxDbi Q9D273.
PRIDEi Q9D273.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031560 ; ENSMUSP00000031560 ; ENSMUSG00000029575 . [Q9D273-1 ]
GeneIDi 77697.
KEGGi mmu:77697.
UCSCi uc008yzo.1. mouse. [Q9D273-1 ]
uc008yzp.1. mouse. [Q9D273-2 ]

Organism-specific databases

CTDi 326625.
MGIi MGI:1924947. Mmab.

Phylogenomic databases

eggNOGi COG2096.
GeneTreei ENSGT00390000008432.
HOGENOMi HOG000291639.
HOVERGENi HBG045589.
KOi K00798.
OMAi FVAARHA.
OrthoDBi EOG7X3QS4.
PhylomeDBi Q9D273.
TreeFami TF312942.

Enzyme and pathway databases

UniPathwayi UPA00148 ; UER00233 .
Reactomei REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.

Miscellaneous databases

NextBioi 347375.
PROi Q9D273.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9D273.
Bgeei Q9D273.
Genevestigatori Q9D273.

Family and domain databases

Gene3Di 1.20.1200.10. 1 hit.
InterProi IPR016030. AdoCbl_synth_CblAdoTrfase-like.
IPR029499. PduO-typ.
[Graphical view ]
Pfami PF01923. Cob_adeno_trans. 1 hit.
[Graphical view ]
ProDomi PD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF89028. SSF89028. 1 hit.
TIGRFAMsi TIGR00636. PduO_Nterm. 1 hit.
ProtoNeti Search...

Publicationsi

  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.
    , 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.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-205 AND LYS-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMMAB_MOUSE
AccessioniPrimary (citable) accession number: Q9D273
Secondary accession number(s): Q3UFL6, Q8CBZ0, Q8VBZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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