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Database: UniProt
Entry: P16332
LinkDB: P16332
Original site: P16332 
ID   MUTA_MOUSE              Reviewed;         748 AA.
AC   P16332; Q3UJU1;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   26-NOV-2014, entry version 120.
DE   RecName: Full=Methylmalonyl-CoA mutase, mitochondrial;
DE            Short=MCM;
DE            EC=5.4.99.2;
DE   AltName: Full=Methylmalonyl-CoA isomerase;
DE   Flags: Precursor;
GN   Name=Mut;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1978672;
RA   Wilkemeyer M.F., Crane A.M., Ledley F.D.;
RT   "Primary structure and activity of mouse methylmalonyl-CoA mutase.";
RL   Biochem. J. 271:449-455(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-341 AND LYS-593, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-210; LYS-333 AND
RP   LYS-600, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Involved in the degradation of several amino acids, odd-
CC       chain fatty acids and cholesterol via propionyl-CoA to the
CC       tricarboxylic acid cycle. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: (R)-methylmalonyl-CoA = succinyl-CoA.
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00666}.
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DR   EMBL; X51941; CAA36204.1; -; mRNA.
DR   EMBL; AK146309; BAE27064.1; -; mRNA.
DR   EMBL; CH466559; EDL23389.1; -; Genomic_DNA.
DR   CCDS; CCDS37618.1; -.
DR   PIR; S08680; S08680.
DR   RefSeq; NP_032676.2; NM_008650.3.
DR   UniGene; Mm.259884; -.
DR   ProteinModelPortal; P16332; -.
DR   SMR; P16332; 34-747.
DR   IntAct; P16332; 2.
DR   MINT; MINT-4102615; -.
DR   PhosphoSite; P16332; -.
DR   MaxQB; P16332; -.
DR   PaxDb; P16332; -.
DR   PRIDE; P16332; -.
DR   Ensembl; ENSMUST00000169611; ENSMUSP00000130941; ENSMUSG00000023921.
DR   GeneID; 17850; -.
DR   KEGG; mmu:17850; -.
DR   UCSC; uc008coo.2; mouse.
DR   CTD; 4594; -.
DR   MGI; MGI:97239; Mut.
DR   eggNOG; COG2185; -.
DR   GeneTree; ENSGT00390000011892; -.
DR   HOGENOM; HOG000003917; -.
DR   HOVERGEN; HBG006423; -.
DR   InParanoid; P16332; -.
DR   KO; K01847; -.
DR   OMA; SIYDMRQ; -.
DR   OrthoDB; EOG78PV8G; -.
DR   TreeFam; TF313557; -.
DR   Reactome; REACT_189075; Defective MMAA causes methylmalonic aciduria type cblA.
DR   Reactome; REACT_189097; Defective MUT causes methylmalonic aciduria mut type.
DR   Reactome; REACT_189118; Cobalamin (Cbl, vitamin B12) transport and metabolism.
DR   Reactome; REACT_253750; Propionyl-CoA catabolism.
DR   ChiTaRS; Mut; mouse.
DR   NextBio; 292593; -.
DR   PRO; PR:P16332; -.
DR   Bgee; P16332; -.
DR   CleanEx; MM_MUT; -.
DR   ExpressionAtlas; P16332; baseline and differential.
DR   Genevestigator; P16332; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IDA:MGI.
DR   GO; GO:0072341; F:modified amino acid binding; IEA:Ensembl.
DR   GO; GO:0050667; P:homocysteine metabolic process; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   Gene3D; 3.20.20.240; -; 1.
DR   Gene3D; 3.40.50.280; -; 1.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR014348; Cbl-dep_enz_cat-sub.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR   InterPro; IPR006098; MMCoA_mutase_a_cat.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF51703; SSF51703; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR   TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cobalamin; Cobalt; Complete proteome; Isomerase;
KW   Metal-binding; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT       1     30       Mitochondrion. {ECO:0000250}.
FT   CHAIN        31    748       Methylmalonyl-CoA mutase, mitochondrial.
FT                                /FTId=PRO_0000019295.
FT   DOMAIN      612    744       B12-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00666}.
FT   METAL       625    625       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000250}.
FT   MOD_RES      87     87       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:23576753}.
FT   MOD_RES     210    210       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:23576753}.
FT   MOD_RES     333    333       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:23576753}.
FT   MOD_RES     341    341       N6-succinyllysine.
FT                                {ECO:0000269|PubMed:23806337}.
FT   MOD_RES     593    593       N6-succinyllysine.
FT                                {ECO:0000269|PubMed:23806337}.
FT   MOD_RES     600    600       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:23576753}.
FT   CONFLICT    256    256       S -> P (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    269    269       A -> T (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    385    385       T -> S (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    407    407       Q -> R (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    491    491       Q -> H (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    499    508       EVLAIDNTSV -> HLLAIDIISL (in Ref. 1;
FT                                CAA36204). {ECO:0000305}.
FT   CONFLICT    561    561       G -> P (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    567    567       L -> F (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    613    614       PR -> LG (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    622    622       Q -> K (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    657    658       QQ -> HD (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
FT   CONFLICT    672    672       L -> H (in Ref. 1; CAA36204).
FT                                {ECO:0000305}.
SQ   SEQUENCE   748 AA;  82844 MW;  DF4A62100A8BD743 CRC64;
     MLRAKNQLFL LSPHYLKQLN IPSASRWKRL LHQQQPLHPE WAVLAKKQLK GKNPEDLIWH
     TPEGISIKPL YSRADTLDLP EELPGVKPFT RGPYPTMYTY RPWTIRQYAG FSTVEESNKF
     YKDNIKAGQQ GLSVAFDLAT HRGYDSDNPR VRGDVGMAGV AIDTVEDTKI LFDGIPLEKM
     SVSMTMNGAV IPVLATFIVT GEEQGVPKEK LTGTIQNDIL KEFMVRNTYI FPPEPSMKII
     ADIFQYTAQH MPKFNSISIS GYHMQEAGAD AILELAYTIA DGLEYCRTGL QAGLTIDEFA
     PRLSFFWGIG MNFYMEIAKM RAGRRLWAHL IEKMFQPKNS KSLLLRAHCQ TSGWSLTEQD
     PYNNIVRTAI EAMAAVFGGT QSLHTNSFDE ALGLPTVKSA RIARNTQIII QEESGIPKVA
     DPWGGSYMME SLTNDVYEAA LKLIYEVEEM GGMAKAVAEG IPKLRIEECA ARRQARIDSG
     SEVIVGVNKY QLEKEDSVEV LAIDNTSVRK KQIEKLKKIK SSRDQALAEQ CLSALTQCAA
     SGDGNILALA VDAARARCTV GEITDALKKV FGEHKANDRM VSGAYRQEFG ESKEITSAIK
     RVNKFMEREG RRPRLLVAKM GQDGHDRGAK VIATGFADLG FDVDIGPLFQ TPREVAQQAV
     DADVHAVGVS TLAAGHKTLV PELIKELTAL GRPDILVMCG GVIPPQDYEF LYEVGVSNVF
     GPGTRIPRAA VQVLDDIEKC LAEKQQSV
//
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