ID   MUTA_CAEEL              Reviewed;         744 AA.
AC   Q23381;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Probable methylmalonyl-CoA mutase, mitochondrial;
DE            EC=5.4.99.2;
DE   AltName: Full=MethylmalonylCoA mutase homolog 1;
DE            Short=MCM;
DE   Flags: Precursor;
GN   Name=mmcm-1; ORFNames=ZK1058.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Involved, in man, in the degradation of several amino
CC       acids, odd-chain fatty acids and cholesterol via propionyl-CoA to
CC       the tricarboxylic acid cycle. MCM has different functions in other
CC       species (By similarity).
CC   -!- CATALYTIC ACTIVITY: (R)-methylmalonyl-CoA = succinyl-CoA.
CC   -!- COFACTOR: Adenosylcobalamin (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC   -!- SIMILARITY: Contains 1 B12-binding domain.
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DR   EMBL; Z35604; CAA84676.2; -; Genomic_DNA.
DR   PIR; T27674; T27674.
DR   RefSeq; NP_497786.2; -.
DR   UniGene; Cel.17830; -.
DR   HSSP; P11653; 1REQ.
DR   IntAct; Q23381; 1.
DR   Ensembl; ZK1058.1; Caenorhabditis elegans.
DR   GeneID; 175503; -.
DR   KEGG; cel:ZK1058.1; -.
DR   WormBase; WBGene00014202; mmcm-1.
DR   WormPep; ZK1058.1; CE30404.
DR   OMA; Q23381; IDSGSEV.
DR   BRENDA; 5.4.99.2; 672.
DR   NextBio; 888440; -.
DR   ArrayExpress; Q23381; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR014348; Cbl-dep_enz_cat-sub.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR006099; MMCoA_mutase_a/b_cat.
DR   InterPro; IPR006098; MMCoA_mutase_a_cat.
DR   Gene3D; G3DSA:3.40.50.280; B12_bd; 1.
DR   Gene3D; G3DSA:3.20.20.240; Cobalamin-dep_enz_cat; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 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; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    744       Probable methylmalonyl-CoA mutase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000019297.
FT   DOMAIN      605    737       B12-binding.
FT   METAL       618    618       Cobalt (cobalamin axial ligand) (By
FT                                similarity).
SQ   SEQUENCE   744 AA;  81683 MW;  599E22008D8FBAEC CRC64;
     MYLQLLKPTL LRCSTRPSSS GAYTRSPIDQ KWAAMAKKAM KGREADTLTW NTPEGIPIKP
     LYLRSDRDCD AQRSVELPGQ FPFTRGPYPT MYTQRPWTIR QYAGFSTVEE SNKFYKENIK
     AGQQGLSVAF DLATHRGYDS DNPRVFGDVG MAGVAVDSVE DMRQLFDGIN LEKMSVSMTM
     NGAVVPVLAM YVVAAEEAGV SRKLLAGTIQ NDILKEFMVR NTYIYPPEPS MRIIGDIFAY
     TSREMPKFNS ISISGYHMQE AGADAVLEMA FTIADGIQYC ETGLNAGLTI DAFAPRLSFF
     WGISMNFYME IAKMRAARRL WANLIKERFS PKSDKSMMLR THSQTSGWSL TEQDPYNNII
     RTTIEAMASV FGGTQSLHTN SFDEALGLPT KFSARIARNT QIIIQEESGI CNVADPWGGS
     YMMESLTDEI YEKALAVIKE IDELGGMAKA VASGMTKLKI EEAAAKKQAR IDAGKDVIVG
     VNKYRLDHEQ QVEVLKIDNA KVREEQCAKL NHIRATRDAE KAQKALDAIT EGARGNGNLM
     ELAIEAARAR CTVGEISDAM EKVFNRHAAV NRLVSGAYKS EFGETSEMSQ VLERVKSFAD
     RDGRQPRIMV AKMGQDGHDR GAKVIATGFA DLGFDVDVGP LFQTPLEAAQ QAVDADVHVI
     GASSLAAGHL TLIPQLIGEL KKLGRPDILV VAGGVIPPQD YKELYDAGVA LVFGPGTRLP
     ACANQILEKL EANLPEAPGK AASR
//