ID F0NE97_SULIR Unreviewed; 415 AA.
AC F0NE97;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=SiRe_0339 {ECO:0000313|EMBL:ADX84433.1};
OS Sulfolobus islandicus (strain REY15A).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=930945 {ECO:0000313|EMBL:ADX84433.1, ECO:0000313|Proteomes:UP000002664};
RN [1] {ECO:0000313|EMBL:ADX84433.1, ECO:0000313|Proteomes:UP000002664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=REY15A {ECO:0000313|EMBL:ADX84433.1,
RC ECO:0000313|Proteomes:UP000002664};
RX PubMed=21278296; DOI=10.1128/JB.01487-10;
RA Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA Huang L., Garrett R.A.;
RT "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT organisms for genetic and virus-host interaction studies.";
RL J. Bacteriol. 193:1672-1680(2011).
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; CP002425; ADX84433.1; -; Genomic_DNA.
DR RefSeq; WP_014513504.1; NC_017276.1.
DR AlphaFoldDB; F0NE97; -.
DR STRING; 930945.SiRe_0339; -.
DR GeneID; 12417234; -.
DR KEGG; sir:SiRe_0339; -.
DR eggNOG; arCOG01608; Archaea.
DR HOGENOM; CLU_002569_5_0_2; -.
DR Proteomes; UP000002664; 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:ADX84433.1}.
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; 46565 MW; 78634078DA70A713 CRC64;
MTEVKKLVEK EVLMNGTQAV AHAAMYADVD VVAAYPIRPY TEVMDTISKL IADGELDAEF
IVAEGEHGQF ETVKHASLAG ARTLVGSSGV GWLYGMEAIV VTATDRAPVV AIIGNRALDD
PGAYGVEHND ALMVRDLGWL LVWVDTAQEA FDTTLIAYRV AEDQRVLLPL GISMDGGFLT
HSEQIVRLPP KELVKNFLPP YNRGKYLVHP DNPITVAPQV NEDWVMEIRR QHEEAIERAR
GVIVEAYEEF KKVFGRYPGS TNELQMPENP FVEPYMVDDA EVVLIGMGTV SKPMKVAIKS
MRRQGYKVGM LRIRWFRPFP TQDVIKYLAN SRVVCVVDRD YSMGSPNRGG VIYHEIRSSL
YDLDQRPRVM SFIGGLGGRE ITIQDVEKII KIGYEHRDTP ITKPVYWVGV RGDPW
//
