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P16332

- MUTA_MOUSE

UniProt

P16332 - MUTA_MOUSE

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Protein
Methylmalonyl-CoA mutase, mitochondrial
Gene
Mut
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle By similarity.

Catalytic activityi

(R)-methylmalonyl-CoA = succinyl-CoA.

Cofactori

Adenosylcobalamin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi625 – 6251Cobalt (cobalamin axial ligand) By similarity

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. methylmalonyl-CoA mutase activity Source: MGI
  4. modified amino acid binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. homocysteine metabolic process Source: Ensembl
  2. post-embryonic development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_189075. Defective MMAA causes methylmalonic aciduria type cblA.
REACT_189097. Defective MUT causes methylmalonic aciduria mut type.
REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA mutase, mitochondrial (EC:5.4.99.2)
Short name:
MCM
Alternative name(s):
Methylmalonyl-CoA isomerase
Gene namesi
Name:Mut
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:97239. Mut.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion By similarity
Add
BLAST
Chaini31 – 748718Methylmalonyl-CoA mutase, mitochondrial
PRO_0000019295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871N6-acetyllysine1 Publication
Modified residuei210 – 2101N6-acetyllysine1 Publication
Modified residuei333 – 3331N6-acetyllysine1 Publication
Modified residuei341 – 3411N6-succinyllysine1 Publication
Modified residuei593 – 5931N6-succinyllysine1 Publication
Modified residuei600 – 6001N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP16332.
PaxDbiP16332.
PRIDEiP16332.

PTM databases

PhosphoSiteiP16332.

Expressioni

Gene expression databases

ArrayExpressiP16332.
BgeeiP16332.
CleanExiMM_MUT.
GenevestigatoriP16332.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP16332. 2 interactions.
MINTiMINT-4102615.

Structurei

3D structure databases

ProteinModelPortaliP16332.
SMRiP16332. Positions 34-747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini612 – 744133B12-binding
Add
BLAST

Sequence similaritiesi

Contains 1 B12-binding domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2185.
GeneTreeiENSGT00390000011892.
HOGENOMiHOG000003917.
HOVERGENiHBG006423.
InParanoidiQ3UJU1.
KOiK01847.
OMAiSIYDMRQ.
OrthoDBiEOG78PV8G.
TreeFamiTF313557.

Family and domain databases

Gene3Di3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProiIPR006159. Acid_CoA_mut_C.
IPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR006099. MeMalonylCoA_mutase_a/b_cat.
IPR006098. MMCoA_mutase_a_cat.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
SUPFAMiSSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16332-1 [UniParc]FASTAAdd to Basket

« Hide

MLRAKNQLFL LSPHYLKQLN IPSASRWKRL LHQQQPLHPE WAVLAKKQLK    50
GKNPEDLIWH TPEGISIKPL YSRADTLDLP EELPGVKPFT RGPYPTMYTY 100
RPWTIRQYAG FSTVEESNKF YKDNIKAGQQ GLSVAFDLAT HRGYDSDNPR 150
VRGDVGMAGV AIDTVEDTKI LFDGIPLEKM SVSMTMNGAV IPVLATFIVT 200
GEEQGVPKEK LTGTIQNDIL KEFMVRNTYI FPPEPSMKII ADIFQYTAQH 250
MPKFNSISIS GYHMQEAGAD AILELAYTIA DGLEYCRTGL QAGLTIDEFA 300
PRLSFFWGIG MNFYMEIAKM RAGRRLWAHL IEKMFQPKNS KSLLLRAHCQ 350
TSGWSLTEQD PYNNIVRTAI EAMAAVFGGT QSLHTNSFDE ALGLPTVKSA 400
RIARNTQIII QEESGIPKVA DPWGGSYMME SLTNDVYEAA LKLIYEVEEM 450
GGMAKAVAEG IPKLRIEECA ARRQARIDSG SEVIVGVNKY QLEKEDSVEV 500
LAIDNTSVRK KQIEKLKKIK SSRDQALAEQ CLSALTQCAA SGDGNILALA 550
VDAARARCTV GEITDALKKV FGEHKANDRM VSGAYRQEFG ESKEITSAIK 600
RVNKFMEREG RRPRLLVAKM GQDGHDRGAK VIATGFADLG FDVDIGPLFQ 650
TPREVAQQAV DADVHAVGVS TLAAGHKTLV PELIKELTAL GRPDILVMCG 700
GVIPPQDYEF LYEVGVSNVF GPGTRIPRAA VQVLDDIEKC LAEKQQSV 748
Length:748
Mass (Da):82,844
Last modified:July 27, 2011 - v2
Checksum:iDF4A62100A8BD743
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561S → P in CAA36204. 1 Publication
Sequence conflicti269 – 2691A → T in CAA36204. 1 Publication
Sequence conflicti385 – 3851T → S in CAA36204. 1 Publication
Sequence conflicti407 – 4071Q → R in CAA36204. 1 Publication
Sequence conflicti491 – 4911Q → H in CAA36204. 1 Publication
Sequence conflicti499 – 50810EVLAIDNTSV → HLLAIDIISL in CAA36204. 1 Publication
Sequence conflicti561 – 5611G → P in CAA36204. 1 Publication
Sequence conflicti567 – 5671L → F in CAA36204. 1 Publication
Sequence conflicti613 – 6142PR → LG in CAA36204. 1 Publication
Sequence conflicti622 – 6221Q → K in CAA36204. 1 Publication
Sequence conflicti657 – 6582QQ → HD in CAA36204. 1 Publication
Sequence conflicti672 – 6721L → H in CAA36204. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51941 mRNA. Translation: CAA36204.1.
AK146309 mRNA. Translation: BAE27064.1.
CH466559 Genomic DNA. Translation: EDL23389.1.
CCDSiCCDS37618.1.
PIRiS08680.
RefSeqiNP_032676.2. NM_008650.3.
UniGeneiMm.259884.

Genome annotation databases

EnsembliENSMUST00000169611; ENSMUSP00000130941; ENSMUSG00000023921.
GeneIDi17850.
KEGGimmu:17850.
UCSCiuc008coo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51941 mRNA. Translation: CAA36204.1 .
AK146309 mRNA. Translation: BAE27064.1 .
CH466559 Genomic DNA. Translation: EDL23389.1 .
CCDSi CCDS37618.1.
PIRi S08680.
RefSeqi NP_032676.2. NM_008650.3.
UniGenei Mm.259884.

3D structure databases

ProteinModelPortali P16332.
SMRi P16332. Positions 34-747.
ModBasei Search...

Protein-protein interaction databases

IntActi P16332. 2 interactions.
MINTi MINT-4102615.

PTM databases

PhosphoSitei P16332.

Proteomic databases

MaxQBi P16332.
PaxDbi P16332.
PRIDEi P16332.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000169611 ; ENSMUSP00000130941 ; ENSMUSG00000023921 .
GeneIDi 17850.
KEGGi mmu:17850.
UCSCi uc008coo.2. mouse.

Organism-specific databases

CTDi 4594.
MGIi MGI:97239. Mut.

Phylogenomic databases

eggNOGi COG2185.
GeneTreei ENSGT00390000011892.
HOGENOMi HOG000003917.
HOVERGENi HBG006423.
InParanoidi Q3UJU1.
KOi K01847.
OMAi SIYDMRQ.
OrthoDBi EOG78PV8G.
TreeFami TF313557.

Enzyme and pathway databases

Reactomei REACT_189075. Defective MMAA causes methylmalonic aciduria type cblA.
REACT_189097. Defective MUT causes methylmalonic aciduria mut type.
REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.

Miscellaneous databases

ChiTaRSi MUT. mouse.
NextBioi 292593.
PROi P16332.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16332.
Bgeei P16332.
CleanExi MM_MUT.
Genevestigatori P16332.

Family and domain databases

Gene3Di 3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProi IPR006159. Acid_CoA_mut_C.
IPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR006099. MeMalonylCoA_mutase_a/b_cat.
IPR006098. MMCoA_mutase_a_cat.
[Graphical view ]
Pfami PF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view ]
SUPFAMi SSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsi TIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEi PS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and activity of mouse methylmalonyl-CoA mutase."
    Wilkemeyer M.F., Crane A.M., Ledley F.D.
    Biochem. J. 271:449-455(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "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].
    Strain: BALB/c.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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-341 AND LYS-593, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "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-87; LYS-210; LYS-333 AND LYS-600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMUTA_MOUSE
AccessioniPrimary (citable) accession number: P16332
Secondary accession number(s): Q3UJU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 117 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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