ID A0A3E2XNN6_9FIRM Unreviewed; 385 AA.
AC A0A3E2XNN6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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 ECO:0000313|EMBL:RGC47659.1};
GN ORFNames=DW747_08290 {ECO:0000313|EMBL:RGC47659.1};
OS Coprococcus catus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=116085 {ECO:0000313|EMBL:RGC47659.1, ECO:0000313|Proteomes:UP000261231};
RN [1] {ECO:0000313|EMBL:RGC47659.1, ECO:0000313|Proteomes:UP000261231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM28-39 {ECO:0000313|EMBL:RGC47659.1,
RC ECO:0000313|Proteomes:UP000261231};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGC47659.1}.
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DR EMBL; QVFD01000006; RGC47659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2XNN6; -.
DR OrthoDB; 6439987at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000261231; 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:UP000261231};
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 385 AA; 41218 MW; 5101CBF51F384185 CRC64;
MIDYRRKTVI KGQQELRCGY TTGTCAAAAA KAAAVTLLSG EICRDVSLQL PGGEHIILET
EFLECSENCV KCGMIKDAGD DPDITNGLLI CAAVEKTEGE TILIDGGMGV GRVTKPGLDQ
PVGAAAINSV PRKMIHEAVE DVRRQYAWEK GLKVTVVIPN GKEKAEKTLN PMLGIVGGLS
VLGTTGIVEP MSEKALIDTI AVDIRMHRAQ NEDILLMAPG NYGLDYLKAA YHIHPDQVIK
ISNFIGDSID LAVCEGASGI VLAGHIGKLI KVAGGIMNTH SHQADARMEI MTAYAAMAGA
GNDILRQIMS SVTTDAGMEI LQQCGLLTET MQLILEKIEA HVKKRAGSQI EIGIIIFSNV
FGMLGQTENV PNLFKKMNAA QHKEE
//
