CBIT_SULIM
ID CBIT_SULIM Reviewed; 199 AA.
AC C3MTW8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=M1425_0110;
OS Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.14.25 / Kamchatka #1;
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}.
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DR EMBL; CP001400; ACP37002.1; -; Genomic_DNA.
DR RefSeq; WP_012710289.1; NC_012588.1.
DR AlphaFoldDB; C3MTW8; -.
DR SMR; C3MTW8; -.
DR EnsemblBacteria; ACP37002; ACP37002; M1425_0110.
DR GeneID; 7813721; -.
DR GeneID; 7939492; -.
DR GeneID; 8759950; -.
DR KEGG; sia:M1425_0110; -.
DR HOGENOM; CLU_094143_0_0_2; -.
DR OMA; RCKFVYA; -.
DR UniPathway; UPA00148; UER00229.
DR Proteomes; UP000001350; 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_1000212932"
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; 22020 MW; D7FB62514DDE4881 CRC64;
MEWKYVIPGI PDNFFERDEE IPMTKEEIRA LALSKLRIRK GDMILDIGCG TGSVTVEASL
LVGSTGKVYG VDKEEKAINL TRRNAEKFGV LNNIVLIKGE APEILFTINE KFDRIFIGGG
SEKIKEIISA SWEIIKKGGR VVIDAILLET VNNAISAMEN IGFMNLEITE VIIAKGMKTK
VGTAMMTRNP IFIISGEKQ
