ID   CBID_PRIMG              Reviewed;         367 AA.
AC   O87693;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 72.
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};
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 509 / CCM 1464 / NBRC 12109;
RX   PubMed=9742225; DOI=10.1042/bj3350159;
RA   Raux E., Lanois A., Warren M.J., Rambach A., Thermes C.;
RT   "Cobalamin (vitamin B12) biosynthesis: identification and characterization
RT   of a Bacillus megaterium cobI operon.";
RL   Biochem. J. 335:159-166(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23922391; DOI=10.1073/pnas.1308098110;
RA   Moore S.J., Lawrence A.D., Biedendieck R., Deery E., Frank S., Howard M.J.,
RA   Rigby S.E., Warren M.J.;
RT   "Elucidation of the anaerobic pathway for the corrin component of cobalamin
RT   (vitamin B12).";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:14906-14911(2013).
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       ECO:0000269|PubMed:23922391}.
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         ECO:0000269|PubMed:23922391};
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; AJ000758; CAA04311.1; -; Genomic_DNA.
DR   PIR; T44687; T44687.
DR   AlphaFoldDB; O87693; -.
DR   SMR; O87693; -.
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   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..367
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_0000141657"
SQ   SEQUENCE   367 AA;  39022 MW;  7989F05E395BDDFA CRC64;
     MKEVPKEPKK LREGYTTGAC ATAATRAALL TLISGEVQDE STIYLPVGRF ATFHLEECEY
     RTSSAVASII KDAGDDPDAT HGALIISEVS WCNGVDIIID GGVGVGRVTK PGLPVPVGEA
     AINPVPRKML KETAQQLLAE YNIQKGVKVV ISVPEGEEMA KKTLNARLGI LGGISILGTR
     GIVVPFSTAA YKASIVQAIS VAKASNCEHV VITTGGRSEK YGMKQFPELP EEAFIQMGDF
     VGFTLKQCKK QGMKKVSLVG MMGKFSKVAQ GVMMVHSKSA PIDFNFLAKA ASESGASAEL
     VEEIKGANTA SQVGDLMTQS GHHQFFEKLC EYCCLSALKE VGDGIDVDTS LYTLKGDFLG
     QAVQHGN