ID A0A1Q2CU90_9ACTN Unreviewed; 378 AA.
AC A0A1Q2CU90;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00787};
DE EC=2.1.1.195 {ECO:0000256|HAMAP-Rule:MF_00787};
DE AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000256|HAMAP-Rule:MF_00787};
GN Name=cbiD {ECO:0000256|HAMAP-Rule:MF_00787};
GN ORFNames=BW733_01290 {ECO:0000313|EMBL:AQP49665.1};
OS Tessaracoccus flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=399497 {ECO:0000313|EMBL:AQP49665.1, ECO:0000313|Proteomes:UP000188235};
RN [1] {ECO:0000313|EMBL:AQP49665.1, ECO:0000313|Proteomes:UP000188235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SST-39T {ECO:0000313|EMBL:AQP49665.1,
RC ECO:0000313|Proteomes:UP000188235};
RX PubMed=18398170; DOI=10.1099/ijs.0.64868-0;
RA Lee D.W., Lee S.D.;
RT "Tessaracoccus flavescens sp. nov., isolated from marine sediment.";
RL Int. J. Syst. Evol. Microbiol. 58:785-789(2008).
CC -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC form cobalt-precorrin-6A. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00787}.
CC -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000256|HAMAP-
CC Rule:MF_00787}.
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DR EMBL; CP019607; AQP49665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2CU90; -.
DR STRING; 399497.BW733_01290; -.
DR KEGG; tfa:BW733_01290; -.
DR OrthoDB; 6439987at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000188235; 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; CbiD-like; 1.
DR HAMAP; MF_00787; CbiD; 1.
DR InterPro; IPR002748; CbiD.
DR InterPro; IPR036074; CbiD_sf.
DR NCBIfam; TIGR00312; cbiD; 1.
DR PANTHER; PTHR35863; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR35863:SF1; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR Pfam; PF01888; CbiD; 1.
DR PIRSF; PIRSF026782; CbiD; 1.
DR SUPFAM; SSF111342; CbiD-like; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00787};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00787}; Reference proteome {ECO:0000313|Proteomes:UP000188235};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00787};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00787}.
SQ SEQUENCE 378 AA; 38526 MW; 11C4C1E94936B1D9 CRC64;
MAEVVGGRRG QLKSSGLRPG WTTGACAAAA ATAAWVALHT GEFPDPVRVL LPKGHDPEFA
LTQEELADGV AMAAVQKDAG DDPDVTHGAV VRARVRRGAP GTGIEFRGGP GVGRVTLPGL
PLAVGEPAIN PGPRGYIAEN LARASARLGV VTDAVVEVSV DGGEELAHRT WNPRIGIEGG
ISILGTTGVV VPYSCSAWID SIRRGVDVAR AAGLTHLAGC TGSTSERVAM QLFGLPELAL
LDMGDFVGAV LKYVSRHQVE RLTLVGGFAK LSKLAAGHLD LHSHRTAVDT THLAELASSA
GASPALAEAV RSANTAMGAL QRCQAGGFPL GDVVAAAARA QGEQVLRGAP VRVGVVCIDR
AGAVVGSAGS PPMRGFDV
//
