ID C3MUL7_SULIM Unreviewed; 297 AA.
AC C3MUL7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=M1425_0371 {ECO:0000313|EMBL:ACP37251.1};
OS Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427317 {ECO:0000313|EMBL:ACP37251.1, ECO:0000313|Proteomes:UP000001350};
RN [1] {ECO:0000313|EMBL:ACP37251.1, ECO:0000313|Proteomes:UP000001350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.14.25 / Kamchatka #1 {ECO:0000313|Proteomes:UP000001350};
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 coenzyme A-dependent oxidative decarboxylation
CC of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-
CC oxobutyrate to form their CoA derivatives.
CC {ECO:0000256|ARBA:ARBA00003908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:42316, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:35179, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342; EC=1.2.7.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000005};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000256|ARBA:ARBA00011631}.
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DR EMBL; CP001400; ACP37251.1; -; Genomic_DNA.
DR RefSeq; WP_012710528.1; NC_012588.1.
DR AlphaFoldDB; C3MUL7; -.
DR GeneID; 84060831; -.
DR KEGG; sia:M1425_0371; -.
DR HOGENOM; CLU_058423_0_0_2; -.
DR Proteomes; UP000001350; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProt.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897:SF1; 2-OXOACID OXIDOREDUCTASE (FERREDOXIN); 1.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 66..201
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT COILED 270..297
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 297 AA; 32932 MW; 2A83667A316BFBE0 CRC64;
MSSLVTPKRI PKFYRGNAAC PGCPIPKELD VLLEVLGNKT VLVVPASCTT IIMGDTSGMP
STVPVIHSAF GAPAAIASGI VRALRTRGDK DVIVTVWAGD GSTGDIGFAS LSGAAERNED
ILYVCYDNEA YMNTGIQRSS LTPKGAWTTT TPEGKREYKK PLPFIIAEHK VPYVATASIA
YIYDYEAKVR KAKQIRGFRY LHLLSPCPPG WRFDSKLTID TAKLAVETGV WPLFEIENGE
FRLTSVSKTL LDKKNRKQVA EYLKLQGRFK QLTEEEIKGI QEEIDEMWEE IKKLVKK
//
