ID   CBID_SYNP6              Reviewed;         374 AA.
AC   Q5N2F9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=syc1321_d;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
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; AP008231; BAD79511.1; -; Genomic_DNA.
DR   RefSeq; WP_011243633.1; NC_006576.1.
DR   AlphaFoldDB; Q5N2F9; -.
DR   SMR; Q5N2F9; -.
DR   STRING; 269084.syc1321_d; -.
DR   EnsemblBacteria; BAD79511; BAD79511; syc1321_d.
DR   KEGG; syc:syc1321_d; -.
DR   eggNOG; COG1903; Bacteria.
DR   OMA; YHGKLIK; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000001175; 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; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..374
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_0000257779"
SQ   SEQUENCE   374 AA;  40693 MW;  583D5B59A93E1D77 CRC64;
     MARSGYTLPV FACAAAIAAL QRLRQPAASI QSVDCHLIDP DQTVAIAIEQ VAPLSPDRAL
     AICRSDPGDN LDLTRGTPIW AEVQLSPRSP DQDSLAIEAG EGIGHSETGP AIYDYAQRLL
     RANLLPLLQT NEQLTVRLIL PEGRRLAERT ANAAFGVVEG LSLLGTHGVA EALSAPEQLQ
     VFRDRLRQLS ADPDLVIFCI GENGLDLSQK IGLPRDRQLK TANWLGPLLV EAGLLGIPRI
     LLFGYHGKLL KLAGSIFHTH HHVADARREI LAAYAIAAGA SLEQVRSLLD FPTVDAATQY
     LDQTDPALAS RLWPQIAEAI VDRSQAYIRR YSEQIPEIGV VLFGRDRQLL TASSQAQTWL
     TNRAIAQPLR YPSA