ID C3N9X0_SULIY Unreviewed; 415 AA.
AC C3N9X0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=YG5714_0361 {ECO:0000313|EMBL:ACP44654.1};
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:ACP44654.1, ECO:0000313|Proteomes:UP000002308};
RN [1] {ECO:0000313|EMBL:ACP44654.1, 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 -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC chain. {ECO:0000256|ARBA:ARBA00011595}.
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DR EMBL; CP001403; ACP44654.1; -; Genomic_DNA.
DR RefSeq; WP_012712944.1; NC_012622.1.
DR AlphaFoldDB; C3N9X0; -.
DR GeneID; 8760189; -.
DR KEGG; siy:YG5714_0361; -.
DR HOGENOM; CLU_002569_5_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 CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:ACP44654.1}.
FT DOMAIN 22..246
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 280..386
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 415 AA; 46596 MW; 0AF83BDD713FBCF6 CRC64;
MTEVKKLVEK EVLMNGTQAV AHAAMYADVD VVAAYPIRPY TEVMDTISKL IADGELDAEF
IVAEGEHGQF ETVKHASLVG ARTLVGSSGV GWLYGMEAIV VTATDRAPVV AIIGNRALDD
PGAYGVEHND ALMVRDVGWL LVWVDTAQEA FDTTLIAYRV AEDQRVLLPL GISMDGGFLT
HSEQIVRLPP KELVKNFLPP YNRGKYLVHP DNPITVAPQV NEDWVMEIRR QHEEAMERAR
GVIVEAYEEF KKVFGRYPGS TNELQMPENP FVEPYMVDDA EVVLIGMGTV SKPMKVAIKS
MRRQGYKVGM LRIRWFRPFP TQDVIKYLAN SRVVCVVDRD YSMGSPNRGG VIYHEIRSSL
YDLDQRPRVM SFIGGLGGRE ITIQDVKKII KIGYEHRDTP ITKPVYWVGV RGDPW
//
