ID   CBID_CLOBA              Reviewed;         381 AA.
AC   B2UXF7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=CLH_2682;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
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; CP001078; ACD51308.1; -; Genomic_DNA.
DR   RefSeq; WP_012449699.1; NC_010723.1.
DR   AlphaFoldDB; B2UXF7; -.
DR   SMR; B2UXF7; -.
DR   KEGG; cbt:CLH_2682; -.
DR   HOGENOM; CLU_041273_1_0_9; -.
DR   OMA; YHGKLIK; -.
DR   OrthoDB; 1282567at2; -.
DR   UniPathway; UPA00148; UER00227.
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..381
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000133733"
SQ   SEQUENCE   381 AA;  41826 MW;  F85ACC06D5EEFFC7 CRC64;
     MFEMYIESGM NKLRCGYTTG SCATGAAKAA TMLLFDLINS EEELNEIEID TPKGIKVEMP
     IDNVVVGKNF VQCTILKFSG DDKDITMGLE IQARVEKIRK EEAEGLSKKL ISNESKTIVL
     DGGIGVGRVT KDGLFVAKGE PAINPVPRQM IIKEIESILP KDKYVKVVIS VPQGTEIGKK
     TFNPRLGIEG GISILGTSGI VYPMSEDALK ASIKLEIKQK SLKSKNLILT FGNLGENYCK
     YLGYKEEEIV ICSNFIGFAL ECCVSCNVKS IIIVGHIGKM SKIAYGCFNT HSRVCGVRLE
     VLALELTLLG YDISLVNKVL NEKTCEGAVK LLGSGYENLY ENIGQKILNS MKTYVYDELK
     IDAVMYYGAS NPILLWSSCL E