ID   CBID_CLOB6              Reviewed;         359 AA.
AC   C3L308;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00787};
DE            EC=2.1.1.195 {ECO:0000255|HAMAP-Rule:MF_00787};
DE   AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000255|HAMAP-Rule:MF_00787};
GN   Name=cbiD {ECO:0000255|HAMAP-Rule:MF_00787}; OrderedLocusNames=CLJ_B0986;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC       form cobalt-precorrin-6A. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26285, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:60063, ChEBI:CHEBI:60064;
CC         EC=2.1.1.195; Evidence={ECO:0000255|HAMAP-Rule:MF_00787};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 6/10. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC   -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00787}.
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DR   EMBL; CP001083; ACQ52459.1; -; Genomic_DNA.
DR   RefSeq; WP_003360895.1; NC_012658.1.
DR   AlphaFoldDB; C3L308; -.
DR   SMR; C3L308; -.
DR   EnsemblBacteria; ACQ52459; ACQ52459; CLJ_B0986.
DR   KEGG; cbi:CLJ_B0986; -.
DR   HOGENOM; CLU_041273_1_0_9; -.
DR   OMA; YHGKLIK; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000002333; Chromosome.
DR   GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2110.10; -; 1.
DR   HAMAP; MF_00787; CbiD; 1.
DR   InterPro; IPR002748; CbiD.
DR   InterPro; IPR036074; CbiD_sf.
DR   PANTHER; PTHR35863; PTHR35863; 1.
DR   Pfam; PF01888; CbiD; 1.
DR   PIRSF; PIRSF026782; CbiD; 1.
DR   SUPFAM; SSF111342; SSF111342; 1.
DR   TIGRFAMs; TIGR00312; cbiD; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..359
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000212935"
SQ   SEQUENCE   359 AA;  39270 MW;  4D1DBFD032EA9980 CRC64;
     MLDLYVNCDG KKLRCGYTTG SCAAAAAKAA AITLFYNKKL EEINIDTPKG IELTIPIEKI
     VVDDNFVECA VIKDGGDDVD ITHGIEIWAR AEKKSSGYAL KGGKGVGVVC GEGLYVPKGE
     PAINPVPRSM IEKEVRSVIS KDSGVEITIF VPKGEEIAKK TFNPRLNIIG GISILGTTGI
     VMPMSEDALK ASIELEINQK TCHGEKELIL LFGNMGEKMA KELNLKENNM VIMSNYVGFA
     LNCCMARKLE KVTIVGHIGK ISKIASGCFN THSRICDTRL ETLALELALM GYDKDLVTKI
     YNQKTTEGAV NLLGEGYEKL YKNLGKKIIR KIEQYTYDSI KADVVMYSMG RGILYSSIE