CBID_PSEU2
ID CBID_PSEU2 Reviewed; 370 AA.
AC Q4ZN23;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=Psyr_4419;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY39449.1; -; Genomic_DNA.
DR RefSeq; WP_011269018.1; NC_007005.1.
DR RefSeq; YP_237487.1; NC_007005.1.
DR AlphaFoldDB; Q4ZN23; -.
DR SMR; Q4ZN23; -.
DR STRING; 205918.Psyr_4419; -.
DR EnsemblBacteria; AAY39449; AAY39449; Psyr_4419.
DR KEGG; psb:Psyr_4419; -.
DR PATRIC; fig|205918.7.peg.4561; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_0_0_6; -.
DR OMA; YHGKLIK; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000000426; 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..370
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000257775"
SQ SEQUENCE 370 AA; 38677 MW; A1BAEB6B16F08CA6 CRC64;
MREETAEQPA PLRSGLTTGS CATATSLAAA RLLLCGQVSD AVEIVLPKGK QVQMRLEFCR
LVDNFAEAAT LKDAGDDPDV THGALVFARV RLQAAAGVRF LAGAGVGTVT RPGLVLAVGE
PAINPVPRRM MTEHLLQLAE EQGYSGGFEV TIGVEGGEAL ALKTMNPRLG ILGGLSILGT
SGIVRPFSCA AYIASIHQGI DVATTNGYRH IAACTGNASE DTMRRVYKIP DIALIEMGDF
VGAVLKHLRR VSVDKLSVCG GFGKISKLAA GHMDLHSRHS SIDLPQLARW AADVGADAGL
QQQILAANTS QQALAMSAAA GVPLGDEVCR HALNFARSIV PASVQVEVFA IDRQGGLVGQ
AGVDSQREIT
