ID A0A415R672_9FIRM Unreviewed; 369 AA.
AC A0A415R672;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 11.
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:RHM54410.1};
GN ORFNames=DWZ54_08785 {ECO:0000313|EMBL:RHM54410.1};
OS Mitsuokella sp. AF33-22.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=2292047 {ECO:0000313|EMBL:RHM54410.1, ECO:0000313|Proteomes:UP000284511};
RN [1] {ECO:0000313|EMBL:RHM54410.1, ECO:0000313|Proteomes:UP000284511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF33-22 {ECO:0000313|EMBL:RHM54410.1,
RC ECO:0000313|Proteomes:UP000284511};
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:RHM54410.1}.
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DR EMBL; QRQA01000012; RHM54410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A415R672; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000284511; 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 369 AA; 39107 MW; D45D0A1390A17F0D CRC64;
MGEKALRGGY TTGACAAAGV KAALLYAQGR PWQVVTLMAL DGTMLTIPVR AVCRTQQGLQ
AEVIKESGDD PDITNGVSVF TTVCRREDEE PMRFAAGEGI GTVTKPGLSV PVGEPSINPG
PRRLMRRAAE DVLGTSAGLS VTIAIPAGRE LARKTLNPVL GIEGGISVIG TTGVLRPMSE
EGFKNSLVPQ IDVALAAGYR DLVFVPGKIG ERLALSWGLP REAIVETSNF IGFLLEAAAD
RHVSRVLLLG HIGKLVKVAA GIFYTHNRIA DARLETMAAY GAAAGLETQD VQRVLASNTT
EDALAVLREA GLLPGVCHTL AERAGERAER YLFGRMQVGV AMMTMQGELL GMNETAEAIG
RDYGWNQKV
//
