ID F0NC30_SULIR Unreviewed; 537 AA.
AC F0NC30;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=SiRe_2028 {ECO:0000313|EMBL:ADX86086.1};
OS Sulfolobus islandicus (strain REY15A).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=930945 {ECO:0000313|EMBL:ADX86086.1, ECO:0000313|Proteomes:UP000002664};
RN [1] {ECO:0000313|EMBL:ADX86086.1, ECO:0000313|Proteomes:UP000002664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=REY15A {ECO:0000313|EMBL:ADX86086.1,
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 -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; CP002425; ADX86086.1; -; Genomic_DNA.
DR RefSeq; WP_014514141.1; NC_017276.1.
DR AlphaFoldDB; F0NC30; -.
DR STRING; 930945.SiRe_2028; -.
DR GeneID; 78428239; -.
DR KEGG; sir:SiRe_2028; -.
DR eggNOG; arCOG03657; Archaea.
DR HOGENOM; CLU_013748_4_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 GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
FT DOMAIN 1..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 383..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 537 AA; 60968 MW; BDD7C85636210A64 CRC64;
MNAGKIFLSL LKESGINKIF IVSGTDYASL IEAKVEDPSL PDFEIVPHEI TAISTAIGYA
LGNKLSAVAV HTTPGTANAL GGIMSAYTSR IPLLVIAGRS PYTEKGSTTS RNLRIHWTQE
ARDQGELVRQ YVKYDFEIRI ADQIPAAISR AIQIMMSEPR GPVYLVLPRE VSVQEVNEVK
RIPMDYYEPA PSPEKINKAK EMLEKSERPV IITWRAGRRK EWFESLRRFA DSYHIPVLNY
AGEVLNYPSN GAMALDRFDL RNADLLLVVE AEVPYFPKKI DLDIPIIKVD VEPSYSYIPY
YGFRCDLCIQ SIPSNFFDYI SIRAKSYDEI RELKIRQEEY KKQEIERLKD RKSIHPKYLS
YEIGNVASEY NLAIFNEYQF NPRYAKLNEF GSYFADLSIG YLGLALGAGV GYKMATNKDV
LITTGDGSFI FGVPEAYYYV SSKYPTMVVI FDNGGWLASA EAVDEVFPEG LAKSKRYYPG
ADFDKRFEIG KTVEAFHGYY ELVEDPWEIK SALIRGLEKV RKENKIAVIQ VIVDKVR
//
