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   03-AUG-2022, entry version 158.
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; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   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 investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Involved, in man, in the degradation of several amino acids,
CC       odd-chain fatty acids and cholesterol via propionyl-CoA to the
CC       tricarboxylic acid cycle. MCM has different functions in other species
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2;
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000305}.
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DR   EMBL; Z35604; CAA84676.2; -; Genomic_DNA.
DR   PIR; T27674; T27674.
DR   RefSeq; NP_497786.2; NM_065385.6.
DR   AlphaFoldDB; Q23381; -.
DR   SMR; Q23381; -.
DR   BioGRID; 40741; 4.
DR   STRING; 6239.ZK1058.1; -.
DR   EPD; Q23381; -.
DR   PaxDb; Q23381; -.
DR   PeptideAtlas; Q23381; -.
DR   EnsemblMetazoa; ZK1058.1.1; ZK1058.1.1; WBGene00014202.
DR   GeneID; 175503; -.
DR   KEGG; cel:CELE_ZK1058.1; -.
DR   UCSC; ZK1058.1.1; c. elegans.
DR   CTD; 175503; -.
DR   WormBase; ZK1058.1; CE30404; WBGene00014202; mmcm-1.
DR   eggNOG; ENOG502QQ7X; Eukaryota.
DR   GeneTree; ENSGT00390000011892; -.
DR   HOGENOM; CLU_009523_3_1_1; -.
DR   InParanoid; Q23381; -.
DR   OMA; PWGGSAY; -.
DR   OrthoDB; 347581at2759; -.
DR   PhylomeDB; Q23381; -.
DR   BRENDA; 5.4.99.2; 1045.
DR   Reactome; R-CEL-71032; Propionyl-CoA catabolism.
DR   Reactome; R-CEL-9759218; Cobalamin (Cbl) metabolism.
DR   PRO; PR:Q23381; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00014202; Expressed in larva and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR   GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IMP:WormBase.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IMP:WormBase.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:WormBase.
DR   GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IBA:GO_Central.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
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   3: Inferred from homology;
KW   Cobalamin; Cobalt; Isomerase; Metal-binding; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..744
FT                   /note="Probable methylmalonyl-CoA mutase, mitochondrial"
FT                   /id="PRO_0000019297"
FT   DOMAIN          605..737
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         618
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
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