CBID_CLOTE
ID CBID_CLOTE Reviewed; 356 AA.
AC Q897K1;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=CTC_00733;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO35335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015927; AAO35335.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_035110292.1; NC_004557.1.
DR AlphaFoldDB; Q897K1; -.
DR SMR; Q897K1; -.
DR STRING; 212717.CTC_00733; -.
DR EnsemblBacteria; AAO35335; AAO35335; CTC_00733.
DR GeneID; 64180521; -.
DR KEGG; ctc:CTC_00733; -.
DR HOGENOM; CLU_041273_1_0_9; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000001412; 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; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..356
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000141663"
SQ SEQUENCE 356 AA; 39050 MW; F7A92D48EC5293DA CRC64;
MLDMYVMVDG KKLRCGYTTG SCATAAAKAA TIMLYNKEKL KTIDIDTPKG VRLHLDIEKI
NIGENYVECC IIKDGGDDPD ATHGMEIWAR AEKKDDGYTL KGGKGVGVVM GEGLYVAKGE
PAINPVPRTM IESEVKSVLP KDRGVEITIF APEGKKVAKK TFNPRLNIIG GISILGTSGI
VMPMSEESLK QSVELEIRQK IANGHKDLIL VFGNIGERKG MEMGLDQSKM VSISNYVGFA
LDCCRGNGVK DITLVGHIGK MCKIAAGCFN THSRVADVRL EVLALELALM GYDIDLVKDV
YNQKTTEGAV KFLGEGYDEL YKRIAEKIAK RIEIYSYGEI SPKILMFSME KILFSE
