ID A0A0C2BDA2_9ACTN Unreviewed; 371 AA.
AC A0A0C2BDA2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=QR77_23685 {ECO:0000313|EMBL:KIF76076.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF76076.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF76076.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF76076.1,
RC ECO:0000313|Proteomes:UP000031584};
RA Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT 150.";
RL Submitted (NOV-2014) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIF76076.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JTHL01000001; KIF76076.1; -; Genomic_DNA.
DR RefSeq; WP_040024143.1; NZ_JTHL01000001.1.
DR AlphaFoldDB; A0A0C2BDA2; -.
DR STRING; 1576605.QR77_23685; -.
DR OrthoDB; 6439987at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000031584; Unassembled WGS sequence.
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:UP000031584};
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 371 AA; 37783 MW; 585BF2DA36C5F57A CRC64;
MSKSASGRDA QLKHTGLRSG WTTGACATAA TTAAYTALLT GDFPDPVTVT LPRGQTPAFA
LAAEKLTGDH AMAAVVKDAG DDPDVTHGAL VRATVRLLPR GAGVVFRAGD GVGTVTRPGL
PLDVGEPAIN PVPRQLMRSH VAEAAARHGG TGDAEITISV DNGAEIARST WNPRLGILGG
LSILGTTGIV VPYSCSAWID SIRRGVDVAL AGGHTHVAGC TGSTSERTVV GAYGLPEEAL
LDMGDFAGAV LKYVRRHPVD RLTICGGFAK LSKLAAGHLD LHSARSQVDK AFLAGLAARA
GAGPDLVAEV AEANTGLAAL QLCQARGVAL GDQVAVTARD EALAVLRGAP VVVDVLCIDR
AGTVVGRSEP R
//
