ID   B0STU6_LEPBP            Unreviewed;       712 AA.
AC   B0STU6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   Name=mutB {ECO:0000313|EMBL:ABZ99630.1};
GN   OrderedLocusNames=LEPBI_II0094 {ECO:0000313|EMBL:ABZ99630.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ99630.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ99630.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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; CP000787; ABZ99630.1; -; Genomic_DNA.
DR   RefSeq; WP_012476568.1; NC_010843.1.
DR   AlphaFoldDB; B0STU6; -.
DR   STRING; 456481.LEPBI_II0094; -.
DR   KEGG; lbi:LEPBI_II0094; -.
DR   HOGENOM; CLU_009523_3_1_12; -.
DR   OrthoDB; 9762378at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS17535-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome II.
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:UniProtKB-EC.
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.
DR   PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABZ99630.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN          580..712
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  78329 MW;  D294B7EBABD941AE CRC64;
     MNKPNFANTP LSFSAPKPDP KSISLWQTAE GISIQSRYQN SDLEGLEHLN YAAGIPPYLR
     GPYSTMYVNK PWTVRQYAGF STAEESNAFY RRNLAAGQKG LSVAFDLATH RGYDSDHERV
     VGDVGKAGVA IDSVLDMKIL FDQIPLDQMS VSMTMNGAVI PVLAFYIVAA EEQGVSKDKL
     SGTIQNDILK EFMVRNTYIY PPKHSMKIIA DIFGYTSKYM PKFNSISISG YHMQEAGATA
     DLELAYTLAD GWEYIKTGIA SGLSVDEFAP RLSFFWAIGM NHFMEIAKMR AGRLLWAKIV
     NQFQPKSTKS LALRTHCQTS GWSLTEQDPF NNVGRTCIEA MAAALGHTQS LHTNALDEAI
     ALPTDFSARI ARNTQIYLQE ETNIHRVIDP WGGSFYVEKL TNDLVHKAWD LITEVQKLGG
     MAEAIETGIP KMRIEEASAR KQARIDSGKD VIVGVNRFRL DKEAPLDILD IDNTAVRIAQ
     IKRLEQMKKD RDNTAVEAAL NAITKCAETG NGNLLELAVD AARKRASLGE ISYAMEKVFG
     RYKAVIRSIS GVYSSEISED KGYIEARNLA DEFAKLEGRR PRIMVAKMGQ DGHDRGAKVI
     STSFADMGFD VDIGPLFQTP AEVAKQVVEN DCHILGVSSL AAGHKTLVPQ VIEELKKLGA
     EDVLVVVGGV IPAQDYDFLY KSGATAIFGP GTVISEAAKQ ILNLLLGERR AA
//