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Entry: CBIC_SALTY
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ID   CBIC_SALTY              Reviewed;         210 AA.
AC   Q05601;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Cobalt-precorrin-8 methylmutase;
DE            EC=5.4.99.60;
DE   AltName: Full=Cobalt-precorrin isomerase;
GN   Name=cbiC; OrderedLocusNames=STM2033;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RC   STRAIN=LT2;
RX   PubMed=8501034; DOI=10.1128/jb.175.11.3303-3316.1993;
RA   Roth J.R., Lawrence J.G., Rubenfield M., Kieffer-Higgins S., Church G.M.;
RT   "Characterization of the cobalamin (vitamin B12) biosynthetic genes of
RT   Salmonella typhimurium.";
RL   J. Bacteriol. 175:3303-3316(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-11.
RX   PubMed=1451790; DOI=10.1016/0014-5793(92)80213-z;
RA   Roessner C.A., Warren M.J., Santander P.J., Atshaves B.P., Ozaki S.,
RA   Stolowich N.J., Iida K., Scott A.I.;
RT   "Expression of 9 Salmonella typhimurium enzymes for cobinamide synthesis.
RT   Identification of the 11-methyl and 20-methyl transferases of corrin
RT   biosynthesis.";
RL   FEBS Lett. 301:73-78(1992).
CC   -!- FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-8X = cob(II)yrinate; Xref=Rhea:RHEA:16209,
CC         ChEBI:CHEBI:58894, ChEBI:CHEBI:70792; EC=5.4.99.60;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 9/10.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CobH/CbiC family. {ECO:0000305}.
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DR   EMBL; L12006; AAA27254.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20937.1; -; Genomic_DNA.
DR   PIR; S21127; S21127.
DR   RefSeq; NP_460978.1; NC_003197.2.
DR   RefSeq; WP_000558988.1; NC_003197.2.
DR   AlphaFoldDB; Q05601; -.
DR   SMR; Q05601; -.
DR   STRING; 99287.STM2033; -.
DR   PaxDb; 99287-STM2033; -.
DR   GeneID; 1253554; -.
DR   KEGG; stm:STM2033; -.
DR   PATRIC; fig|99287.12.peg.2155; -.
DR   HOGENOM; CLU_084703_1_1_6; -.
DR   OMA; GAPIFCD; -.
DR   PhylomeDB; Q05601; -.
DR   BioCyc; MetaCyc:MONOMER-13227; -.
DR   BioCyc; SENT99287:STM2033-MONOMER; -.
DR   UniPathway; UPA00148; UER00230.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0043778; F:cobalt-precorrin-8 methylmutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016993; F:precorrin-8X methylmutase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.10230; Cobalamin biosynthesis CobH/CbiC, precorrin-8X methylmutase; 1.
DR   InterPro; IPR003722; Cbl_synth_CobH/CbiC.
DR   InterPro; IPR036588; CobH/CbiC_sf.
DR   PANTHER; PTHR43588; COBALT-PRECORRIN-8 METHYLMUTASE; 1.
DR   PANTHER; PTHR43588:SF1; COBALT-PRECORRIN-8 METHYLMUTASE; 1.
DR   Pfam; PF02570; CbiC; 1.
DR   SUPFAM; SSF63965; Precorrin-8X methylmutase CbiC/CobH; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Direct protein sequencing; Isomerase;
KW   Reference proteome.
FT   CHAIN           1..210
FT                   /note="Cobalt-precorrin-8 methylmutase"
FT                   /id="PRO_0000135923"
FT   ACT_SITE        45
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  23034 MW;  C2098D0EB84BDDA5 CRC64;
     MHYIQQPQTI EANSFTIISD IIRETRPDYR FASPLHEAII KRVIHTTADF DWLDILWFSA
     DALEQLCDAL RHPCIIYTDT TMALSGINKR LLATFGGECR CYISDPRVVR AAQTQGITRS
     MAAVDIAIAE EEKNKLFVFG NAPTALFRLL EHNVTVSGVV GVPVGFVGAA ESKEALTHSH
     FPAVAALGRK GGSNVAAAIV NALLYHLREA
//
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