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CBIT_SACS2
ID   CBIT_SACS2              Reviewed;         199 AA.
AC   Q97WC7;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=SSO2303;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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; AE006641; AAK42461.1; -; Genomic_DNA.
DR   PIR; F90400; F90400.
DR   RefSeq; WP_009991808.1; NC_002754.1.
DR   AlphaFoldDB; Q97WC7; -.
DR   SMR; Q97WC7; -.
DR   STRING; 273057.SSO2303; -.
DR   EnsemblBacteria; AAK42461; AAK42461; SSO2303.
DR   GeneID; 44128031; -.
DR   KEGG; sso:SSO2303; -.
DR   PATRIC; fig|273057.12.peg.2393; -.
DR   eggNOG; arCOG00977; Archaea.
DR   HOGENOM; CLU_094143_0_0_2; -.
DR   InParanoid; Q97WC7; -.
DR   OMA; RCKFVYA; -.
DR   PhylomeDB; Q97WC7; -.
DR   UniPathway; UPA00148; UER00229.
DR   Proteomes; UP000001974; 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; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..199
FT                   /note="Probable cobalt-precorrin-6B C(15)-methyltransferase
FT                   (decarboxylating)"
FT                   /id="PRO_0000134944"
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;  21799 MW;  6DE834AA6C1C105F CRC64;
     MEWNYVIPGI PDNLFERDEE IPMTKEEIRA LALSKLRIKK GDKVLDIGCG TGSITVEASL
     LVGNSGRVYG IDKEEKAINL TRRNAEKFGV LNNIVLIKGE APAILSTINE KFDRIFIGGG
     SEKIKEIISA SWEIINKGGR IVIDAILLET VNNALSAMEK IGFVNLEITE VIIAKGMKTK
     VGTAMMARNP IFIISGEKP
 
 
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