ID   E0XUY9_9GAMM            Unreviewed;       717 AA.
AC   E0XUY9;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
OS   uncultured gamma proteobacterium HF0200_40H22.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; environmental samples.
OX   NCBI_TaxID=710985 {ECO:0000313|EMBL:ADI18230.1};
RN   [1] {ECO:0000313|EMBL:ADI18230.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x;
RA   Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.;
RT   "Time-series analyses of Monterey Bay coastal microbial picoplankton using
RT   a 'genome proxy' microarray.";
RL   Environ. Microbiol. 13:116-134(2011).
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000256|ARBA:ARBA00008465}.
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DR   EMBL; GU474884; ADI18230.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0XUY9; -.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:InterPro.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   CDD; cd03679; MM_CoA_mutase_alpha_like; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
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   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR   PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          585..717
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   717 AA;  78227 MW;  2C4BAF30AFDCE5C3 CRC64;
     MNDSTDQSLK SWQNLATREL AGGKPEDLEW ATPEGISIKP LYTREDLEAL DHQDGLPGFP
     PYVRGPRATM YAGRPWTIRQ YSGFSTAEES NAFYRRNLAA GQSGLSVAFD LATHRGYDSD
     HPRVTGDIGM AGVAIDSVED MRILFDGIPL DRMSVSMTMN GAVIPILAMF IVAGEEQGVD
     KASLSGTLQN DILKEFMVRN TYIYPPQESM RIVSDIIGYT AVHMPRFNPI SISGYHIQEA
     GATSVQELAY TLADGVEYVR TAVASGLEID KFAPRLSFFF GIGMNFFMEV AKLRAARLLW
     AQLIKEKFDP SDPRSLMLRT HCQTSGVSLT SEDPYNNIVR TTIEALAAVF GGTQSLHTNS
     FDEALALPTD FSAHIARNTQ LILQEEAGIN RVVDPLGGSY YVESLTASLV AQARSLIDEV
     EDMGGMTQAI INGIPKMRIE EAAARRQARI DRGEEVVVGV NRYESLEEAE VDILSIDNSE
     VLKTQVDRLE SVRENRDDAK CQHALEALKT AAGRSGANLL EYAVEAARAR ATVGEISLVL
     EAEFGRYQAQ VRTISGVYGE AYQQDETFQL LRKDVDAFAG QQGRRPRILV AKLGQDGHDR
     GARIIATGFA DVGFDVDIGP LFQTPEEVVQ QALDNDVHVI GVSSQAAGHS TLVPKVLETL
     LEREAGHIKV VLGGVVPKVD REALAALGVA AFFGPGTPIL GAAREVFDLI PRTQEGD
//