CBID_PSEPG
ID CBID_PSEPG Reviewed; 364 AA.
AC B0KK08;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=PputGB1_4887;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABZ00772.1; -; Genomic_DNA.
DR RefSeq; WP_012274403.1; NC_010322.1.
DR AlphaFoldDB; B0KK08; -.
DR SMR; B0KK08; -.
DR STRING; 76869.PputGB1_4887; -.
DR EnsemblBacteria; ABZ00772; ABZ00772; PputGB1_4887.
DR KEGG; ppg:PputGB1_4887; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_0_0_6; -.
DR OMA; YHGKLIK; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000002157; 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..364
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000083593"
SQ SEQUENCE 364 AA; 37775 MW; D38681FDC1E6B8BB CRC64;
MREETREQPA PLRSGLTTGS CATATSLAAA RLLLSGETSD AVSITLPKGK VVQMRLEFCR
LAGESAEAGT LKDAGDDPDV THGALLYSQV RLLDEPSIRF VAGSGVGTVT RPGLVLAVGE
PAINPVPRRM ISEHLQRLAD ECGYFGGFEV TVNVQGGEQL ALKTMNPRLG ILGGLSILGT
SGIVRPFSCA AYIASIHQGI DVAHTNGYTH IAACTGNASE DTMRRVYGLP EIALIEMGDF
VGAVLKHLRK VPVPRLTLCG GFGKISKLAA GHMDLHSRHS SIDLPQLAGW AADIGADAAL
QAAIIGANTS QQALALAHAA GIALGDAVCA HALAFARSVV PAQVQVEVFA IDRQGGIVGR
AGVQ
