(data stored in ACNUC7421 zone)

SWISSPROT: CBIT_SULIK

ID   CBIT_SULIK              Reviewed;         199 AA.
AC   C4KJM8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 44.
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};
GN   OrderedLocusNames=M164_0112;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
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-
CC       7. {ECO:0000255|HAMAP-Rule:MF_00786}.
CC   -!- CATALYTIC ACTIVITY: Cobalt-precorrin-6B + S-adenosyl-L-methionine
CC       = cobalt-precorrin-7 + S-adenosyl-L-homocysteine + CO(2).
CC       {ECO:0000255|HAMAP-Rule:MF_00786}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic
CC       route): step 8/10. {ECO:0000255|HAMAP-Rule:MF_00786}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Archaeal-type CbiT family. {ECO:0000255|HAMAP-Rule:MF_00786}.
DR   EMBL; CP001402; ACR40748.1; -; Genomic_DNA.
DR   RefSeq; WP_012710289.1; NC_012726.1.
DR   ProteinModelPortal; C4KJM8; -.
DR   SMR; C4KJM8; -.
DR   EnsemblBacteria; ACR40748; ACR40748; M164_0112.
DR   GeneID; 8759950; -.
DR   KEGG; sid:M164_0112; -.
DR   HOGENOM; HOG000290407; -.
DR   KO; K02191; -.
DR   OMA; RCKFVYA; -.
DR   OrthoDB; POG093Z07LQ; -.
DR   BioCyc; SISL426118:GI01-112-MONOMER; -.
DR   UniPathway; UPA00148; UER00229.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02469; CbiT; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KJM8.
DR   SWISS-2DPAGE; C4KJM8.
KW   Cobalamin biosynthesis; Complete proteome; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    199       Probable cobalt-precorrin-6B C(15)-
FT                                methyltransferase (decarboxylating).
FT                                /FTId=PRO_1000212930.
FT   REGION       48     52       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00786}.
FT   BINDING      24     24       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00786}.
FT   BINDING      72     72       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00786}.
FT   BINDING     101    101       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00786}.
SQ   SEQUENCE   199 AA;  22020 MW;  D7FB62514DDE4881 CRC64;
     MEWKYVIPGI PDNFFERDEE IPMTKEEIRA LALSKLRIRK GDMILDIGCG TGSVTVEASL
     LVGSTGKVYG VDKEEKAINL TRRNAEKFGV LNNIVLIKGE APEILFTINE KFDRIFIGGG
     SEKIKEIISA SWEIIKKGGR VVIDAILLET VNNAISAMEN IGFMNLEITE VIIAKGMKTK
     VGTAMMTRNP IFIISGEKQ
//

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