ID A0A1H2VIQ4_9FIRM Unreviewed; 376 AA.
AC A0A1H2VIQ4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=SAMN05216391_11427 {ECO:0000313|EMBL:SDW67824.1};
OS Lachnospiraceae bacterium KHCPX20.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1855375 {ECO:0000313|EMBL:SDW67824.1, ECO:0000313|Proteomes:UP000199590};
RN [1] {ECO:0000313|EMBL:SDW67824.1, ECO:0000313|Proteomes:UP000199590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHCPX20 {ECO:0000313|EMBL:SDW67824.1,
RC ECO:0000313|Proteomes:UP000199590};
RA de Groot N.N.;
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; FNOC01000014; SDW67824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2VIQ4; -.
DR STRING; 1855375.SAMN05216391_11427; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000199590; 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:UP000199590};
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 376 AA; 41200 MW; 0EDF2FFD4F771439 CRC64;
MAYYFTTGSC SAAAAKAAAY MLLSGQKKES IVITTPKGID FHAELLNISI REDQVSCGVL
KDGGEDPDVT TGYIITATVS YLPDHDQRET KAKDCPHIQI DGGEGVGRVH RPGLDQPVGN
AAINSVPRQM IQREVREVMN LFDCHRSLKV IISVPGGEKL AKRTFNPRLG IEGGISILGT
SGIVEPMSTK ALLDTIRVQL HQKHVLGKKK LVISPGNYGL DFMRTTYGYD LEEAVKCSNY
IGETLEIVAS EQFTHVLLCG HMGKLIKLAG GIMNTHSAEA DCRIELMVNA ALAVGLPVPM
LRKMQECIST DAAYQILVDA NLTDEFMDYL IRKIKFYLDK RVAGRFTIEC IVFSNEFGLM
GKTAGADQLL KELKDE
//
