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P16332 (MUTA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonyl-CoA mutase, mitochondrial

Short name=MCM
EC=5.4.99.2
Alternative name(s):
Methylmalonyl-CoA isomerase
Gene names
Name:Mut
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length748 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Adenosylcobalamin.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the methylmalonyl-CoA mutase family.

Contains 1 B12-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion By similarity
Chain31 – 748718Methylmalonyl-CoA mutase, mitochondrial
PRO_0000019295

Regions

Domain612 – 744133B12-binding

Sites

Metal binding6251Cobalt (cobalamin axial ligand) By similarity

Amino acid modifications

Modified residue871N6-acetyllysine Ref.5
Modified residue2101N6-acetyllysine Ref.5
Modified residue3331N6-acetyllysine Ref.5
Modified residue3411N6-succinyllysine Ref.4
Modified residue5931N6-succinyllysine Ref.4
Modified residue6001N6-acetyllysine Ref.5

Experimental info

Sequence conflict2561S → P in CAA36204. Ref.1
Sequence conflict2691A → T in CAA36204. Ref.1
Sequence conflict3851T → S in CAA36204. Ref.1
Sequence conflict4071Q → R in CAA36204. Ref.1
Sequence conflict4911Q → H in CAA36204. Ref.1
Sequence conflict499 – 50810EVLAIDNTSV → HLLAIDIISL in CAA36204. Ref.1
Sequence conflict5611G → P in CAA36204. Ref.1
Sequence conflict5671L → F in CAA36204. Ref.1
Sequence conflict613 – 6142PR → LG in CAA36204. Ref.1
Sequence conflict6221Q → K in CAA36204. Ref.1
Sequence conflict657 – 6582QQ → HD in CAA36204. Ref.1
Sequence conflict6721L → H in CAA36204. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16332 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: DF4A62100A8BD743

FASTA74882,844
        10         20         30         40         50         60 
MLRAKNQLFL LSPHYLKQLN IPSASRWKRL LHQQQPLHPE WAVLAKKQLK GKNPEDLIWH 

        70         80         90        100        110        120 
TPEGISIKPL YSRADTLDLP EELPGVKPFT RGPYPTMYTY RPWTIRQYAG FSTVEESNKF 

       130        140        150        160        170        180 
YKDNIKAGQQ GLSVAFDLAT HRGYDSDNPR VRGDVGMAGV AIDTVEDTKI LFDGIPLEKM 

       190        200        210        220        230        240 
SVSMTMNGAV IPVLATFIVT GEEQGVPKEK LTGTIQNDIL KEFMVRNTYI FPPEPSMKII 

       250        260        270        280        290        300 
ADIFQYTAQH MPKFNSISIS GYHMQEAGAD AILELAYTIA DGLEYCRTGL QAGLTIDEFA 

       310        320        330        340        350        360 
PRLSFFWGIG MNFYMEIAKM RAGRRLWAHL IEKMFQPKNS KSLLLRAHCQ TSGWSLTEQD 

       370        380        390        400        410        420 
PYNNIVRTAI EAMAAVFGGT QSLHTNSFDE ALGLPTVKSA RIARNTQIII QEESGIPKVA 

       430        440        450        460        470        480 
DPWGGSYMME SLTNDVYEAA LKLIYEVEEM GGMAKAVAEG IPKLRIEECA ARRQARIDSG 

       490        500        510        520        530        540 
SEVIVGVNKY QLEKEDSVEV LAIDNTSVRK KQIEKLKKIK SSRDQALAEQ CLSALTQCAA 

       550        560        570        580        590        600 
SGDGNILALA VDAARARCTV GEITDALKKV FGEHKANDRM VSGAYRQEFG ESKEITSAIK 

       610        620        630        640        650        660 
RVNKFMEREG RRPRLLVAKM GQDGHDRGAK VIATGFADLG FDVDIGPLFQ TPREVAQQAV 

       670        680        690        700        710        720 
DADVHAVGVS TLAAGHKTLV PELIKELTAL GRPDILVMCG GVIPPQDYEF LYEVGVSNVF 

       730        740 
GPGTRIPRAA VQVLDDIEKC LAEKQQSV 

« Hide

References

« Hide 'large scale' references
[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. 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].
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51941 mRNA. Translation: CAA36204.1.
AK146309 mRNA. Translation: BAE27064.1.
CH466559 Genomic DNA. Translation: EDL23389.1.
PIRS08680.
RefSeqNP_032676.2. NM_008650.3.
UniGeneMm.259884.

3D structure databases

ProteinModelPortalP16332.
SMRP16332. Positions 34-747.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP16332. 2 interactions.
MINTMINT-4102615.

PTM databases

PhosphoSiteP16332.

Proteomic databases

PaxDbP16332.
PRIDEP16332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000169611; ENSMUSP00000130941; ENSMUSG00000023921.
GeneID17850.
KEGGmmu:17850.
UCSCuc008coo.2. mouse.

Organism-specific databases

CTD4594.
MGIMGI:97239. Mut.

Phylogenomic databases

eggNOGCOG2185.
GeneTreeENSGT00390000011892.
HOGENOMHOG000003917.
HOVERGENHBG006423.
InParanoidQ3UJU1.
KOK01847.
OMAAQDVYNN.
OrthoDBEOG78PV8G.
TreeFamTF313557.

Gene expression databases

ArrayExpressP16332.
BgeeP16332.
CleanExMM_MUT.
GenevestigatorP16332.

Family and domain databases

Gene3D3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProIPR006159. 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]
PfamPF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
SUPFAMSSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMUT. mouse.
NextBio292593.
PROP16332.
SOURCESearch...

Entry information

Entry nameMUTA_MOUSE
AccessionPrimary (citable) accession number: P16332
Secondary accession number(s): Q3UJU1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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