ID A0A371IZ82_9FIRM Unreviewed; 381 AA.
AC A0A371IZ82;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=CHL78_016425 {ECO:0000313|EMBL:RDY25792.1};
OS Romboutsia weinsteinii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=2020949 {ECO:0000313|EMBL:RDY25792.1, ECO:0000313|Proteomes:UP000215694};
RN [1] {ECO:0000313|EMBL:RDY25792.1, ECO:0000313|Proteomes:UP000215694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19649 {ECO:0000313|EMBL:RDY25792.1,
RC ECO:0000313|Proteomes:UP000215694};
RX PubMed=28982987;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Cantin P., Raymond F.,
RA Corbeil J., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of Romboutsia weinsteinii sp. nov. Strain CCRI-
RT 19649(T) Isolated from Surface Water.";
RL Genome Announc. 5:e00901-17(2017).
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:RDY25792.1}.
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DR EMBL; NOJY02000047; RDY25792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371IZ82; -.
DR OrthoDB; 6439987at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000215694; 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:UP000215694};
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 381 AA; 42373 MW; 9BC41BE30B66A681 CRC64;
MEEYVYIDGK KYRRGYTTGS CAAAASKAAT HMLFAKEKIE IINIDTPKGI PLSLKVRNIN
ICSDYVECSI EKDGGDDIDA THTMHIFARA EFVDREEDDI IVDGGIGVGV VTKKGLSVEV
GRPAINPVPM RMIHTEVRKV IGDDFKNNIG SDKSIKLTIY APEGVEIAKK TFNPRLGIIG
GISILGTTGI VEPMSDEGWK KSLSIELEMK KAQGLDKIIL VPGNHGEQFI KEKLGLDMKY
VVRTSNFIGY MLKEAKRIGY KKILMAGHIG KYIKISAGIF NTHSKIADAR NEIMIANLAM
MRAPYEFLEK INECVTTEGA VELINDSEYI SIYDSISNKC KAKIDQYLLD EEINVEVMIF
SMDKSLLGKS DHSDELVEVF R
//
