ID   CBID_MOOTA              Reviewed;         365 AA.
AC   Q2RJI7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Moth_1088;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC19402.1; -; Genomic_DNA.
DR   RefSeq; WP_011392602.1; NC_007644.1.
DR   RefSeq; YP_429945.1; NC_007644.1.
DR   AlphaFoldDB; Q2RJI7; -.
DR   SMR; Q2RJI7; -.
DR   STRING; 264732.Moth_1088; -.
DR   EnsemblBacteria; ABC19402; ABC19402; Moth_1088.
DR   GeneID; 61289781; -.
DR   KEGG; mta:Moth_1088; -.
DR   PATRIC; fig|264732.11.peg.1169; -.
DR   eggNOG; COG1903; Bacteria.
DR   HOGENOM; CLU_041273_1_0_9; -.
DR   OMA; YHGKLIK; -.
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..365
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_0000257767"
SQ   SEQUENCE   365 AA;  38642 MW;  5A9EA6ED4EEC9D67 CRC64;
     MVQKLRRGYT TGTCAAGAAK AAALALWRGE EVQEITLTLP RGEIITLPVT VHKGVEEAEA
     IIIKDAGDDP DVTHGVAIHV RARKQAGGIT LRGGEGIGIV TRPGLAVPVG EPAINPVPRA
     MIKEAVAAIV PPGLGMELEI SIPEGARLAR RTLNPRLGIE GGLSILGTTG IVEPMSEEAF
     RNSLVPQIDV ALAAGWETLV LTPGRLGQRQ AEEKYGLPAT AIILTSNFIG YLLEACVERR
     VKRVLLWGHG GKLVKVAGGI FYTHSHVADA RQEIIAALAA AAGASREIVQ QILAATTVEA
     VQEVIRGSDF EPGFWDSLAA RASQRATDLV HGELTVGTAL LNLQGDIMGR DEVARQIMGD
     WGYDR