ID D2PH41_SULID Unreviewed; 632 AA.
AC D2PH41;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=LD85_2802 {ECO:0000313|EMBL:ADB88406.1};
OS Sulfolobus islandicus (strain L.D.8.5 / Lassen #2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=425944 {ECO:0000313|EMBL:ADB88406.1, ECO:0000313|Proteomes:UP000001404};
RN [1] {ECO:0000313|Proteomes:UP000001404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.D.8.5 / Lassen #2 {ECO:0000313|Proteomes:UP000001404};
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; CP001731; ADB88406.1; -; Genomic_DNA.
DR RefSeq; WP_012714478.1; NC_013769.1.
DR AlphaFoldDB; D2PH41; -.
DR GeneID; 8762640; -.
DR KEGG; sii:LD85_2802; -.
DR HOGENOM; CLU_017038_1_0_2; -.
DR Proteomes; UP000001404; 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 Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR NCBIfam; NF041170; Oxoac_fdxalpha_Archa; 1.
DR PANTHER; PTHR32154:SF16; PYRUVATE FLAVODOXIN_FERREDOXIN OXIDOREDUCTASE DOMAIN PROTEIN; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:ADB88406.1}.
FT DOMAIN 12..212
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 242..491
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 518..586
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 632 AA; 70219 MW; A81A1E0AB31C05CA CRC64;
MRISWMIGGA QGSGVDTSAN IFGNAVAASG YYIYGNREYY SNIKGRHSYF NLTISDKPPR
SIAQQVEILT SFDAETIFQH FNEVKDVLIY STEVESTKAE QVQSMEPEIT EHVIKFLKEK
GYGTTVRDVI NYLKKEKGVK VIPIDYMEIL KKVADQAKVQ LSVADRARNT IAIAASYKLL
GLREQYLLNS ITRTFRQEVF AKINTIASQL AMQPIQPMYN LPELPNNEEK INLDGNTAAA
IGKIYGGLRF QSYYPITPAS DESVFIEAHQ TVFTVDPKTG EKRKSTIVVV QAEDELAAIN
MASGAALTGV RAATATSGPG FSLMVEGMGW AGMNEVPVVI TYYIRGGPST GQPTRTSQAD
LMFALNAGHG EFPRIVIASG DHVEAFHDGT WALNLAQKYQ TPVIHLVDKA LANSYSIIPK
KQLGMENIRV EKGKIVINSS TPELKRFEIT EDGISPFAPL GTTRIHYTGD EHDEYGFIAE
ASENREKMYE KRIKKLFTAD KEIPEENRVN IFGNTDSKIA IITWGSPKGA ILDAMEELES
EGIKPMLIQI RMFSPFPKNL MKKLLSGREF IIDVESNYFG QAGEVLKLNT GIEPTHHILK
WNGRPMMRDE VKEAIKAVVQ KGERKVVLHG GA
//
