ID F0NN59_SULIH Unreviewed; 297 AA.
AC F0NN59;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=SiH_0372 {ECO:0000313|EMBL:ADX81742.1};
OS Sulfolobus islandicus (strain HVE10/4).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX81742.1, ECO:0000313|Proteomes:UP000006395};
RN [1] {ECO:0000313|EMBL:ADX81742.1, ECO:0000313|Proteomes:UP000006395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX81742.1,
RC ECO:0000313|Proteomes:UP000006395};
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}.
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DR EMBL; CP002426; ADX81742.1; -; Genomic_DNA.
DR RefSeq; WP_012712962.1; NC_017275.1.
DR AlphaFoldDB; F0NN59; -.
DR GeneID; 8760220; -.
DR KEGG; sih:SiH_0372; -.
DR HOGENOM; CLU_058423_0_0_2; -.
DR Proteomes; UP000006395; 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; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897:SF1; 2-OXOACID OXIDOREDUCTASE (FERREDOXIN); 1.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 66..201
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT COILED 270..297
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 297 AA; 32901 MW; CBC6737A316BFBE1 CRC64;
MSSLVTPKRI PKFYRGNAAC PGCPIPKELD VLLEVLGNKT VLVVPASCTT IIMGDTSGMP
STVPVIHSAF GAPAAIASGI VRALRTRGDK DVIVTVWAGD GSTGDIGFAS LSGAAERNED
ILYVCYDNEA YMNTGIQRSS LTPKGAWTTT TPEGKREYKK PLPFIIAEHK VPYVATASIA
YIYDYEAKVR KAKQIRGFRY LHLLSPCPPG WRFDSKLTID TAKLAVETGV WPLFEIENGE
FRLTSVSKTL LDKKNRKPVA EYLKLQGRFK QLTEEEIKGI QEEIDEMWEE IKKLVKK
//
