ID   CBIT_SULIN              Reviewed;         199 AA.
AC   C3NJQ5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=YN1551_0110;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001404; ACP47307.1; -; Genomic_DNA.
DR   RefSeq; WP_012716954.1; NC_012623.1.
DR   AlphaFoldDB; C3NJQ5; -.
DR   SMR; C3NJQ5; -.
DR   EnsemblBacteria; ACP47307; ACP47307; YN1551_0110.
DR   GeneID; 7811484; -.
DR   KEGG; sin:YN1551_0110; -.
DR   HOGENOM; CLU_094143_0_0_2; -.
DR   OMA; RCKFVYA; -.
DR   UniPathway; UPA00148; UER00229.
DR   Proteomes; UP000006818; 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; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02469; CbiT; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..199
FT                   /note="Probable cobalt-precorrin-6B C(15)-methyltransferase
FT                   (decarboxylating)"
FT                   /id="PRO_1000212933"
FT   BINDING         24
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         48..52
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         72
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
SQ   SEQUENCE   199 AA;  22002 MW;  D7FB6257E1B48881 CRC64;
     MEWKYVIPGI PDNFFERDEE IPMTKEEIRA LALSKLRIRK GDMILDIGCG TGSVTVEASL
     LVGSTGKVYG VDKEEKAINL TRRNAEKFGV LNNIVLIKGE APEILFTINE KFDRIFIGGG
     SEKIKEIISA SWEIIKKGGR VVIDAILLET VNNAISAMEN IGFINLEITE VIIAKGMKTK
     VGTAMMTRNP IFIISGEKQ