CBID_CLONN
ID CBID_CLONN Reviewed; 358 AA.
AC A0Q345;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=NT01CX_0581;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61369.1; -; Genomic_DNA.
DR RefSeq; WP_011723026.1; NC_008593.1.
DR AlphaFoldDB; A0Q345; -.
DR SMR; A0Q345; -.
DR STRING; 386415.NT01CX_0581; -.
DR EnsemblBacteria; ABK61369; ABK61369; NT01CX_0581.
DR KEGG; cno:NT01CX_0581; -.
DR PATRIC; fig|386415.7.peg.2085; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_1_0_9; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000008220; 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..358
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000046856"
SQ SEQUENCE 358 AA; 39328 MW; F3F9E5C3D024BA3B CRC64;
MFEMYVDCDG KKLRCGYTTG SCAAAAAKAA TRMLYYGGKL EKITIDIPKG IEITVPIGNI
EVGEDYVKCS VTKFSGDDPD ITNGIEIYAT ARKIESGYSL KGGKGVGVVM GEGLYVKKGE
PAINPVPRQM IQKEVMEIVP KDKGIEITIS VPKGEEIAKK TFNPRLNIEG GISILGTTGI
VTPMSEDALK ESIALEIKQK YASGVTRPVL VFGNMGEERA KALGFNKNDM IIVSNYIGYA
LDICRQKEIK SIALVGHIGK MCKIASGCFQ THSRVCDVRM ETIALELALM NAPFHIVNEV
YNMKTTEGAV KFLEDKYSEV YLRIAQKIKS RIYTYTYDTI DAEIVMFSME KGVIARVN
