ID A0A1I6XCT9_9ACTN Unreviewed; 360 AA.
AC A0A1I6XCT9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05660657_00376 {ECO:0000313|EMBL:SFT35644.1};
OS Geodermatophilus amargosae.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1296565 {ECO:0000313|EMBL:SFT35644.1, ECO:0000313|Proteomes:UP000199546};
RN [1] {ECO:0000313|Proteomes:UP000199546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46136 {ECO:0000313|Proteomes:UP000199546};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FPBA01000001; SFT35644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6XCT9; -.
DR STRING; 1296565.SAMN05660657_00376; -.
DR OrthoDB; 6439987at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000199546; 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};
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 360 AA; 36616 MW; 47AC9DDD31795B80 CRC64;
MSRDGASGLR HGWTTGACAT AATTAAYTAL LTGDFPDPVT IDLPGGRHPS FALSREGLDE
GGAWAGVVKD AGDDPDVTHG ALVSVRVTHG EPGGGVVFRA GEGVGTVTKP GLPLAVGEPA
INPMPRQFMR EHVAAVAQRH GGSGDVVVEV SIEDGAELAR RTWNPRLGIL GGLSVLGTTG
VVVPYSCSSW IDSIRRGIDV ARAAGHEHVA GCTGSTSERT VQELHGLPED ALLDMGDFAG
AVLKYLRRHP VPRLTVAGGI GKLAKLADGH LDLHSGRSQV SFDSLAARVA AAGGSPRLVE
GVRGANTALD ALRQCQAAGL PLGDLVAAGA RETALGVLLG APVAVDVVVI DRAGTIVGRA
//
