ID   CBID_SYNY3              Reviewed;         378 AA.
AC   P73423;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   25-MAY-2022, entry version 118.
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=slr1538;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA17463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000022; BAA17463.1; ALT_INIT; Genomic_DNA.
DR   PIR; S77360; S77360.
DR   AlphaFoldDB; P73423; -.
DR   SMR; P73423; -.
DR   IntAct; P73423; 1.
DR   STRING; 1148.1652542; -.
DR   PaxDb; P73423; -.
DR   EnsemblBacteria; BAA17463; BAA17463; BAA17463.
DR   KEGG; syn:slr1538; -.
DR   eggNOG; COG1903; Bacteria.
DR   InParanoid; P73423; -.
DR   OMA; YHGKLIK; -.
DR   PhylomeDB; P73423; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000001425; 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; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..378
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_0000141687"
SQ   SEQUENCE   378 AA;  40799 MW;  9DE79332BB53F12A CRC64;
     MSQSISAQSG YTLPVFACAS AIAAVETLLT SNCPDSVTLE LLEPARTAEI AIEQGALLGH
     HRALAITRSE PGNNLDLTRH TPVWAEVEFT PGEGKLIIQG GEGIGKQLDR EGQAAIYSYA
     QRLLRHHLQP YISGDQTLMV SLILPLGRTL ATRTSNAAFG VVEGLSLLGT SGIAQPLSAP
     EQLAEFQQHL TSAAQQHQCL VFCLGENGLD LARQWGVPLD QMVKTANWLG SLFVAAAAVG
     VQEILLLGYH GKLIKLAGGI FHTHHHLADG RLEILTAQAV QAGLPYPLVQ ELGQAPTTEA
     GLKLLRHWQT EQNCPWVSKI YQAMADTVDR RSEEYVYKVS QHQLKVGSLL FDGDRQPVAI
     STQGQAMADK LGMTIPET