ID M9UCL9_SULIS Unreviewed; 400 AA.
AC M9UCL9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=SiL_2402 {ECO:0000313|EMBL:AGJ63838.1};
OS Sulfolobus islandicus LAL14/1.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1241935;
RN [1] {ECO:0000313|EMBL:AGJ63838.1, ECO:0000313|Proteomes:UP000013006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAL14/1 {ECO:0000313|EMBL:AGJ63838.1};
RX PubMed=23594878; DOI=10.1098/rsob.130010;
RA Jaubert C., Danioux C., Oberto J., Cortez D., Bize A., Krupovic M., She Q.,
RA Forterre P., Prangishvili D., Sezonov G.;
RT "Genomics and genetics of Sulfolobus islandicus LAL14/1, a model
RT hyperthermophilic archaeon.";
RL Open Biol. 3:130010-130010(2013).
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; CP003928; AGJ63838.1; -; Genomic_DNA.
DR RefSeq; WP_012719216.1; NC_021058.1.
DR AlphaFoldDB; M9UCL9; -.
DR GeneID; 84062854; -.
DR KEGG; sic:SiL_2402; -.
DR HOGENOM; CLU_002569_5_0_2; -.
DR Proteomes; UP000013006; 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:SF30; 2-OXOACID OXIDOREDUCTASE (FERREDOXIN); 1.
DR PANTHER; PTHR32154; 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:AGJ63838.1}.
FT DOMAIN 15..237
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 263..363
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 400 AA; 44703 MW; 99E06CBFA7B4B406 CRC64;
MIRKVISGNE AVALGVKLAR VGVTGIYPIT PQTTIIEKLA EMRAKGEIET EIVRVESEHS
AMAATFGAAL GGVRAFTATA SQGLLYMHEM IWWVAGSRVP VVMVVGTRAV GAPWNIWNEH
TDFTSERDSG WIMAFASNPQ EALDLTLQAF RISEDERVFL PMMVGMDGFI LSHTKTNVLI
PDQDQVDEFL PPRRQPYVID PEDPIGMGNI FPPEGYMRLR ESIDLALRNS ENIIKEIGRE
YNKKINPLGD YSTLNVSYKL EDADYAIVLM GAWAGDAMEA VDTLREKGIK IGMLRIRYLR
PWSEKEIRNA LKDKRAVLVL DRSTSFGRGG GPLYVEVKST ISDIVPQVKG VVSGLGGVTV
NKSELLYIFN KFVEGLKDDV IWYYPKEVGK IEFRTPRDIE
//
