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 03-APR-2013, entry version 107.
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.
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: (R)-methylmalonyl-CoA = succinyl-CoA.
CC -!- COFACTOR: Adenosylcobalamin.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC -!- SIMILARITY: Contains 1 B12-binding domain.
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DR EMBL; X51941; CAA36204.1; -; mRNA.
DR EMBL; AK146309; BAE27064.1; -; mRNA.
DR EMBL; CH466559; EDL23389.1; -; Genomic_DNA.
DR IPI; IPI00133553; -.
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 PhosphoSite; P16332; -.
DR PaxDb; P16332; -.
DR PRIDE; P16332; -.
DR Ensembl; ENSMUST00000169611; ENSMUSP00000130941; ENSMUSG00000023921.
DR GeneID; 17850; -.
DR KEGG; mmu:17850; -.
DR CTD; 4594; -.
DR MGI; MGI:97239; Mut.
DR eggNOG; COG2185; -.
DR GeneTree; ENSGT00390000011892; -.
DR HOGENOM; HOG000003917; -.
DR HOVERGEN; HBG006423; -.
DR InParanoid; Q3UJU1; -.
DR KO; K01847; -.
DR OMA; NDVHILG; -.
DR OrthoDB; EOG45X7VJ; -.
DR ChiTaRS; MUT; mouse.
DR NextBio; 292593; -.
DR ArrayExpress; P16332; -.
DR Bgee; P16332; -.
DR CleanEx; MM_MUT; -.
DR Genevestigator; P16332; -.
DR GermOnline; ENSMUSG00000023921; Mus musculus.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:Compara.
DR GO; GO:0050667; P:homocysteine metabolic process; IEA:Compara.
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; SSF52242; Cbl-bd; 1.
DR SUPFAM; SSF51703; Cbl-dep_enz_cat; 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 2: Evidence at transcript level;
KW Cobalamin; Cobalt; Complete proteome; Isomerase; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1 30 Mitochondrion (By similarity).
FT CHAIN 31 748 Methylmalonyl-CoA mutase, mitochondrial.
FT /FTId=PRO_0000019295.
FT DOMAIN 612 744 B12-binding.
FT METAL 625 625 Cobalt (cobalamin axial ligand) (By
FT similarity).
FT CONFLICT 256 256 S -> P (in Ref. 1; CAA36204).
FT CONFLICT 269 269 A -> T (in Ref. 1; CAA36204).
FT CONFLICT 385 385 T -> S (in Ref. 1; CAA36204).
FT CONFLICT 407 407 Q -> R (in Ref. 1; CAA36204).
FT CONFLICT 491 491 Q -> H (in Ref. 1; CAA36204).
FT CONFLICT 499 508 EVLAIDNTSV -> HLLAIDIISL (in Ref. 1;
FT CAA36204).
FT CONFLICT 561 561 G -> P (in Ref. 1; CAA36204).
FT CONFLICT 567 567 L -> F (in Ref. 1; CAA36204).
FT CONFLICT 613 614 PR -> LG (in Ref. 1; CAA36204).
FT CONFLICT 622 622 Q -> K (in Ref. 1; CAA36204).
FT CONFLICT 657 658 QQ -> HD (in Ref. 1; CAA36204).
FT CONFLICT 672 672 L -> H (in Ref. 1; CAA36204).
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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