ID   CBIT_SULTO              Reviewed;         192 AA.
AC   Q96ZL5; F9VNM9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00786};
DE            EC=2.1.1.196 {ECO:0000255|HAMAP-Rule:MF_00786};
GN   Name=cbiT {ECO:0000255|HAMAP-Rule:MF_00786}; OrderedLocusNames=STK_18190;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
CC   -!- FUNCTION: Catalyzes the methylation of C-15 in cobalt-precorrin-6B
CC       followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
CC       {ECO:0000255|HAMAP-Rule:MF_00786}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 +
CC         CO2 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36067,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:70791, ChEBI:CHEBI:72780; EC=2.1.1.196;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00786};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 8/10. {ECO:0000255|HAMAP-Rule:MF_00786}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Archaeal-type
CC       CbiT family. {ECO:0000255|HAMAP-Rule:MF_00786}.
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DR   EMBL; BA000023; BAK54675.1; -; Genomic_DNA.
DR   RefSeq; WP_010979887.1; NC_003106.2.
DR   AlphaFoldDB; Q96ZL5; -.
DR   SMR; Q96ZL5; -.
DR   STRING; 273063.STK_18190; -.
DR   EnsemblBacteria; BAK54675; BAK54675; STK_18190.
DR   GeneID; 1459875; -.
DR   KEGG; sto:STK_18190; -.
DR   PATRIC; fig|273063.9.peg.2075; -.
DR   eggNOG; arCOG00977; Archaea.
DR   OMA; RCKFVYA; -.
DR   OrthoDB; 82864at2157; -.
DR   UniPathway; UPA00148; UER00229.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0043776; F:cobalt-precorrin-6B C5-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00786; CbiT; 1.
DR   InterPro; IPR023475; CbiT.
DR   InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02469; CbiT; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..192
FT                   /note="Probable cobalt-precorrin-6B C(15)-methyltransferase
FT                   (decarboxylating)"
FT                   /id="PRO_0000134945"
FT   BINDING         20
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         44..48
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
SQ   SEQUENCE   192 AA;  21072 MW;  EB7DE8CF2AAA8AF2 CRC64;
     MRLPGIPDEE FIRVEKIPMT KEEIRVLALS KARLFDGAKF IDIGSGTGSV TVEAGLVVGE
     KGKVWAIEKD KDAVELTKKN VEKFKLNNVV IIEGEAPEAL DHVDSEVDAI FIGGTERLEE
     ILLSSDKKLK NGGRIVIDAI LLETVNKALS TLNQMGYKTD VIEVIIAKGM KTSKGYAMIS
     RNPIFIVYGE KP