CBID_METS3
ID CBID_METS3 Reviewed; 361 AA.
AC A5ULG4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00787};
DE EC=2.1.1.195 {ECO:0000255|HAMAP-Rule:MF_00787};
DE AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000255|HAMAP-Rule:MF_00787};
GN Name=cbiD {ECO:0000255|HAMAP-Rule:MF_00787}; OrderedLocusNames=Msm_0837;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC form cobalt-precorrin-6A. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00787}.
CC -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000255|HAMAP-
CC Rule:MF_00787}.
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DR EMBL; CP000678; ABQ87042.1; -; Genomic_DNA.
DR RefSeq; WP_004033091.1; NC_009515.1.
DR AlphaFoldDB; A5ULG4; -.
DR SMR; A5ULG4; -.
DR STRING; 420247.Msm_0837; -.
DR EnsemblBacteria; ABQ87042; ABQ87042; Msm_0837.
DR GeneID; 5217266; -.
DR KEGG; msi:Msm_0837; -.
DR PATRIC; fig|420247.28.peg.834; -.
DR eggNOG; arCOG04383; Archaea.
DR HOGENOM; CLU_041273_1_0_2; -.
DR OMA; YHGKLIK; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000001992; Chromosome.
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; -; 1.
DR HAMAP; MF_00787; CbiD; 1.
DR InterPro; IPR002748; CbiD.
DR InterPro; IPR036074; CbiD_sf.
DR PANTHER; PTHR35863; PTHR35863; 1.
DR Pfam; PF01888; CbiD; 1.
DR PIRSF; PIRSF026782; CbiD; 1.
DR SUPFAM; SSF111342; SSF111342; 1.
DR TIGRFAMs; TIGR00312; cbiD; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..361
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000062247"
SQ SEQUENCE 361 AA; 39375 MW; 73B03397F7A72A8C CRC64;
MTNENYTGVT TGTIATACSL AALESILDTS DIDCVKVKTP KKTLDIIIDE CKRLSHSSAC
AVAHKNPYND PDVTVGLAIV ATVELLDKTS DGDSVIITGG EGVGKITKPG LQIPVGEYAI
NPVPRRMIRK NLERILPEDK VAKVTISIPE GRKIAKKTMN PKLGIVGGIS VIGTTGIARS
MSSEAYKNSI VTQIDVALAL NLDNLVFVPG NIGEKLALKQ LDITKQHIIQ TGNYVGFMFE
EAKKRGIDEF TFFGHIGKLI KIAGGIFNTK HAIADGRREI MITHAGICGA DTKTLQKLYD
SKTTEDMLDI LDEENLHLDV CNSIALAIKE RCMQRFDLDL NVILVDMEGN YLNDNFERFL
L
