ID E0E2E0_9FIRM Unreviewed; 388 AA.
AC E0E2E0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 05-FEB-2025, entry version 49.
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:EFM64974.1};
GN ORFNames=HMPREF0634_1270 {ECO:0000313|EMBL:EFM64974.1};
OS Peptostreptococcus stomatis DSM 17678.
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Peptostreptococcaceae; Peptostreptococcus.
OX NCBI_TaxID=596315 {ECO:0000313|EMBL:EFM64974.1, ECO:0000313|Proteomes:UP000003244};
RN [1] {ECO:0000313|EMBL:EFM64974.1, ECO:0000313|Proteomes:UP000003244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17678 {ECO:0000313|EMBL:EFM64974.1,
RC ECO:0000313|Proteomes:UP000003244};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFM64974.1}.
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DR EMBL; ADGQ01000035; EFM64974.1; -; Genomic_DNA.
DR AlphaFoldDB; E0E2E0; -.
DR STRING; 596315.HMPREF0634_1270; -.
DR eggNOG; COG1903; Bacteria.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000003244; Unassembled WGS sequence.
DR GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
DR GO; GO:0019251; P:anaerobic cobalamin 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:UP000003244};
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 388 AA; 42369 MW; F19B385070488401 CRC64;
MIDEFVYVDG KKYRRGYTSG SCACGATKAA LIMLLEKRNI NEVRIGTPKG VDLDLKIDNI
SREKGWVQCS VKKDGGDDID ATHGMDIFAR LELVQADQVP DFRSDLDSDY LFITSGQGIG
RVTKKGLDIR PGRPAINRVP LKMILKEVQE TLDEAGLDIY DYLGGRKILV TIFAPQGQEI
AKRTFNSNLG IEGGISIIGT TGIVEPMSDE GWKKALSAEL AIKRAEGRET IILVPGNIGR
DIMAKSYGAD LDGIVKMSNF IGYMLMETKR LGFKKVIIGG HIGKLIKLSG GITNSHSRVA
DARSEIMVAN LALLGAPLEL LKEVDACLST DAMVDIIRDA GYSKVFKVLA DKAASKAKVY
MRLGQEDHMD IEVYLFSMDG SLLAKSQI
//
