ID C3N921_SULIY Unreviewed; 543 AA.
AC C3N921;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=YG5714_2277 {ECO:0000313|EMBL:ACP46526.1};
OS Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=439386 {ECO:0000313|EMBL:ACP46526.1, ECO:0000313|Proteomes:UP000002308};
RN [1] {ECO:0000313|EMBL:ACP46526.1, ECO:0000313|Proteomes:UP000002308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.G.57.14 / Yellowstone #1 {ECO:0000313|Proteomes:UP000002308};
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}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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; CP001403; ACP46526.1; -; Genomic_DNA.
DR AlphaFoldDB; C3N921; -.
DR KEGG; siy:YG5714_2277; -.
DR HOGENOM; CLU_013748_4_0_2; -.
DR Proteomes; UP000002308; 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; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
FT DOMAIN 7..132
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 389..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 543 AA; 61726 MW; 38942A2691869B71 CRC64;
MIKYQDMNAG KIFLSLLKES GINKIFIVSG TDYASLIEAK VEDPSLPDFE IVPHEITAIS
TAIGYALGNK LSAVAVHTTP GTANALGGIM SAYTSRIPLL VIAGRSPYTE KGSTASRNLR
IHWTQEARDQ GELVRQYVKY DFEIRMADQI PAAISRAIQI MMSEPRGPVY LVLPREVSIQ
EVNEVKRIPM DYYEPAPSPE KINKAKEMLE KSERPVIITW RAGRRKEWFE SLRRFADSYN
IPVLNYAGEV LNYPSNGAMA LDRFDLRNAD LLLVVEAEVP YFPKKIDLDI PIIKVDVEPS
YSYIPYYGFR CDLCIQSIPS NFFDYISIRA KSYDEIRELK IRQEEYKKQE IERLKDRKSI
HPKYLSYEIG NVASEYNLAI FNEYQFNPRY AKLNEFGSYF ADLSIGYLGL ALGAGVGYKM
ATNKDVLITT GDGSFIFGVP EAYYYVSSKY PTMVVIFDNG GWLASAEAVD EVFPEGLAKS
KRYYPGADFD KRFEIGKTVE AFHGYYELVE DPWEIKSALI RGLEKVRKEN KIAVIQVIVD
KVR
//
