ID   CBID_PICTO              Reviewed;         341 AA.
AC   Q3V8B2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=PTO0110;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT42695.1; -; Genomic_DNA.
DR   RefSeq; WP_011176911.1; NC_005877.1.
DR   AlphaFoldDB; Q3V8B2; -.
DR   SMR; Q3V8B2; -.
DR   STRING; 263820.PTO0110; -.
DR   EnsemblBacteria; AAT42695; AAT42695; PTO0110.
DR   GeneID; 2844474; -.
DR   KEGG; pto:PTO0110; -.
DR   PATRIC; fig|263820.9.peg.124; -.
DR   eggNOG; arCOG04383; Archaea.
DR   HOGENOM; CLU_041273_0_0_2; -.
DR   OMA; YHGKLIK; -.
DR   OrthoDB; 57676at2157; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000000438; 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..341
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_0000257788"
SQ   SEQUENCE   341 AA;  36506 MW;  4410E78C8B6210AC CRC64;
     MPRYGYTTGT CATAATRAAI IALATGRKLK SVEVKLPSKK NAIININDVE IKEDYAMASV
     VKDGGDDPDV TTGLVIYSKV SFTDSGIYVD GGEGIGRVTK EGLPVKPGNA AINPVPMRMI
     KNTAMETLSE LNISSGLKII ISAPGGDKVA LKTCNPKLGI IGGISILGTT GIVVPYSAAS
     WRASIVLAMR VAIKSNYDTV ILTTGSRTEE YARKLFNDRY PCIDVGDFIG FSIRRAAENG
     IKNIIIACMP GKASKLAMGM EDTSSRNSGV DFDFIYKMAL SINIKNAEII KNSNTVNALV
     DEFTDDGLFK LMAELAKINL RRISNINIDV IIFDMSGNVI S