CBID_SYNE7
ID CBID_SYNE7 Reviewed; 374 AA.
AC Q31RU7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=Synpcc7942_0190;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000100; ABB56222.1; -; Genomic_DNA.
DR RefSeq; WP_011243633.1; NC_007604.1.
DR AlphaFoldDB; Q31RU7; -.
DR SMR; Q31RU7; -.
DR STRING; 1140.Synpcc7942_0190; -.
DR PRIDE; Q31RU7; -.
DR EnsemblBacteria; ABB56222; ABB56222; Synpcc7942_0190.
DR KEGG; syf:Synpcc7942_0190; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_1_2_3; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0190-MON; -.
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..374
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000257783"
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
