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Protein

Methylmalonyl-CoA mutase, mitochondrial

Gene

Mut

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

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: MGI

GO - Biological processi

  1. homocysteine metabolic process Source: MGI
  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.
REACT_253750. Propionyl-CoA catabolism.

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 – 3030MitochondrionBy similarityAdd
BLAST
Chaini31 – 748718Methylmalonyl-CoA mutase, mitochondrialPRO_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

BgeeiP16332.
CleanExiMM_MUT.
ExpressionAtlasiP16332. baseline and differential.
GenevestigatoriP16332.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP16332. 2 interactions.
MINTiMINT-4102615.

Structurei

3D structure databases

ProteinModelPortaliP16332.
SMRiP16332. Positions 34-747.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini612 – 744133B12-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the methylmalonyl-CoA mutase family.Curated
Contains 1 B12-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2185.
GeneTreeiENSGT00390000011892.
HOGENOMiHOG000003917.
HOVERGENiHBG006423.
InParanoidiP16332.
KOiK01847.
OMAiYCRTGLK.
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

        10         20         30         40         50
MLRAKNQLFL LSPHYLKQLN IPSASRWKRL LHQQQPLHPE WAVLAKKQLK
60 70 80 90 100
GKNPEDLIWH TPEGISIKPL YSRADTLDLP EELPGVKPFT RGPYPTMYTY
110 120 130 140 150
RPWTIRQYAG FSTVEESNKF YKDNIKAGQQ GLSVAFDLAT HRGYDSDNPR
160 170 180 190 200
VRGDVGMAGV AIDTVEDTKI LFDGIPLEKM SVSMTMNGAV IPVLATFIVT
210 220 230 240 250
GEEQGVPKEK LTGTIQNDIL KEFMVRNTYI FPPEPSMKII ADIFQYTAQH
260 270 280 290 300
MPKFNSISIS GYHMQEAGAD AILELAYTIA DGLEYCRTGL QAGLTIDEFA
310 320 330 340 350
PRLSFFWGIG MNFYMEIAKM RAGRRLWAHL IEKMFQPKNS KSLLLRAHCQ
360 370 380 390 400
TSGWSLTEQD PYNNIVRTAI EAMAAVFGGT QSLHTNSFDE ALGLPTVKSA
410 420 430 440 450
RIARNTQIII QEESGIPKVA DPWGGSYMME SLTNDVYEAA LKLIYEVEEM
460 470 480 490 500
GGMAKAVAEG IPKLRIEECA ARRQARIDSG SEVIVGVNKY QLEKEDSVEV
510 520 530 540 550
LAIDNTSVRK KQIEKLKKIK SSRDQALAEQ CLSALTQCAA SGDGNILALA
560 570 580 590 600
VDAARARCTV GEITDALKKV FGEHKANDRM VSGAYRQEFG ESKEITSAIK
610 620 630 640 650
RVNKFMEREG RRPRLLVAKM GQDGHDRGAK VIATGFADLG FDVDIGPLFQ
660 670 680 690 700
TPREVAQQAV DADVHAVGVS TLAAGHKTLV PELIKELTAL GRPDILVMCG
710 720 730 740
GVIPPQDYEF LYEVGVSNVF GPGTRIPRAA VQVLDDIEKC LAEKQQSV
Length:748
Mass (Da):82,844
Last modified:July 27, 2011 - v2
Checksum:iDF4A62100A8BD743
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561S → P in CAA36204. (PubMed:1978672)Curated
Sequence conflicti269 – 2691A → T in CAA36204. (PubMed:1978672)Curated
Sequence conflicti385 – 3851T → S in CAA36204. (PubMed:1978672)Curated
Sequence conflicti407 – 4071Q → R in CAA36204. (PubMed:1978672)Curated
Sequence conflicti491 – 4911Q → H in CAA36204. (PubMed:1978672)Curated
Sequence conflicti499 – 50810EVLAIDNTSV → HLLAIDIISL in CAA36204. (PubMed:1978672)Curated
Sequence conflicti561 – 5611G → P in CAA36204. (PubMed:1978672)Curated
Sequence conflicti567 – 5671L → F in CAA36204. (PubMed:1978672)Curated
Sequence conflicti613 – 6142PR → LG in CAA36204. (PubMed:1978672)Curated
Sequence conflicti622 – 6221Q → K in CAA36204. (PubMed:1978672)Curated
Sequence conflicti657 – 6582QQ → HD in CAA36204. (PubMed:1978672)Curated
Sequence conflicti672 – 6721L → H in CAA36204. (PubMed:1978672)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP16332.
SMRiP16332. Positions 34-747.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16332. 2 interactions.
MINTiMINT-4102615.

PTM databases

PhosphoSiteiP16332.

Proteomic databases

MaxQBiP16332.
PaxDbiP16332.
PRIDEiP16332.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4594.
MGIiMGI:97239. Mut.

Phylogenomic databases

eggNOGiCOG2185.
GeneTreeiENSGT00390000011892.
HOGENOMiHOG000003917.
HOVERGENiHBG006423.
InParanoidiP16332.
KOiK01847.
OMAiYCRTGLK.
OrthoDBiEOG78PV8G.
TreeFamiTF313557.

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.
REACT_253750. Propionyl-CoA catabolism.

Miscellaneous databases

ChiTaRSiMut. mouse.
NextBioi292593.
PROiP16332.
SOURCEiSearch...

Gene expression databases

BgeeiP16332.
CleanExiMM_MUT.
ExpressionAtlasiP16332. baseline and differential.
GenevestigatoriP16332.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 122 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.