CBID_SYNC1
ID CBID_SYNC1 Reviewed; 350 AA.
AC Q3A7A9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-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}; OrderedLocusNames=Pcar_0475;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-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; CP000142; ABA87735.1; -; Genomic_DNA.
DR RefSeq; WP_011340159.1; NC_007498.2.
DR AlphaFoldDB; Q3A7A9; -.
DR SMR; Q3A7A9; -.
DR STRING; 338963.Pcar_0475; -.
DR EnsemblBacteria; ABA87735; ABA87735; Pcar_0475.
DR KEGG; pca:Pcar_0475; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_1_0_7; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000002534; 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..350
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000257768"
SQ SEQUENCE 350 AA; 36753 MW; 89721915D1B4EEE9 CRC64;
MAGLQGGFTT GACAAAAAKM AAALLCGEAI SERISIPLLD GTRESLPLAY AHRLPDGAEA
AVYKNAGDDP DVTNGALIIA RVVASDKPLE FRAGEGVGII TKPGLALPPG EPAINPGPRL
MIESAVREVT DRGLRVTIAI PDGKQLAERT FNPRLGIKGG ISVLGTTGRV RPFSLEAVRK
TMECSYNVAC ASGVRHPVLV PGHIGERAAH RHFQVTQEQV VEAGNEWGFM IDLVAQTPPS
ALLVLGHPGK LAKLPLGHWD THSSRSASPV PSVRELATRI LECPVAESTT VEGVFADLTA
EQRQCLGDTL ARALQIAVSH RLDHRAPVAT ALINLAGDML GSCGDLTPWQ
