ID   CBID_LEPBJ              Reviewed;         369 AA.
AC   Q04NF4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=LBJ_4180;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000351; ABJ77566.1; -; Genomic_DNA.
DR   RefSeq; WP_011671370.1; NC_008511.1.
DR   AlphaFoldDB; Q04NF4; -.
DR   SMR; Q04NF4; -.
DR   PRIDE; Q04NF4; -.
DR   EnsemblBacteria; ABJ77566; ABJ77566; LBJ_4180.
DR   KEGG; lbj:LBJ_4180; -.
DR   HOGENOM; CLU_041273_0_0_12; -.
DR   OMA; YHGKLIK; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000000656; Chromosome 2.
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..369
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000046859"
SQ   SEQUENCE   369 AA;  39525 MW;  9EEF122441FFD3FB CRC64;
     MSTKELREGF TTGACSAAAA KAATRLLLKG EPVLEIETTL PNDRQVLFPV KRCQLEGEVA
     ICSVVKDAGD DPDCTHGAEL TARVRLTKES KIVLKGGDGV ATVTKTGLGI EVGEPAINPI
     PRKNISEMIL EELKGSSFNG AEVEISVPGG QEMAKKTMNK RLGLIGGISI IGTTGIVKPF
     STAAFKASVI QAIRMAREYE VDTVILTTGG KSEKFAMNLF PNLKELSFIQ AGDFIGTGIK
     TSVKEFIRHV IVVGMIGKLS KMADGVMMTH RGGSSVNTKM LSDIARSVGI PEPIAIDIQN
     ANTARHALEI CKENGYEIIT TKICEIVARN CSKHAGTNMS ISCYMVDFDG TLLGKFENFS
     QKSKLRKGI