ID F0QYW8_VULM7 Unreviewed; 277 AA.
AC F0QYW8;
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=VMUT_0032 {ECO:0000313|EMBL:ADY00249.1};
OS Vulcanisaeta moutnovskia (strain 768-28).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=985053 {ECO:0000313|EMBL:ADY00249.1, ECO:0000313|Proteomes:UP000007485};
RN [1] {ECO:0000313|EMBL:ADY00249.1, ECO:0000313|Proteomes:UP000007485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-28 {ECO:0000313|EMBL:ADY00249.1,
RC ECO:0000313|Proteomes:UP000007485};
RX PubMed=21398550; DOI=10.1128/JB.00237-11;
RA Gumerov V.M., Mardanov A.V., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of 'Vulcanisaeta moutnovskia' strain 768-28, a
RT novel member of the hyperthermophilic crenarchaeal genus vulcanisaeta.";
RL J. Bacteriol. 193:2355-2356(2011).
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; CP002529; ADY00249.1; -; Genomic_DNA.
DR RefSeq; WP_013603413.1; NC_015151.1.
DR AlphaFoldDB; F0QYW8; -.
DR STRING; 985053.VMUT_0032; -.
DR GeneID; 10287684; -.
DR KEGG; vmo:VMUT_0032; -.
DR eggNOG; arCOG01599; Archaea.
DR HOGENOM; CLU_048564_2_0_2; -.
DR OrthoDB; 30755at2157; -.
DR Proteomes; UP000007485; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate 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; cd03375; TPP_OGFOR; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR PANTHER; PTHR48084:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 76..206
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 277 AA; 30589 MW; 1E808B0667344F56 CRC64;
MNPLIQKYLR SEYAQGKRRT IFCPGCGNGI ILGYFVRAID ELKHEGRFDD SKLYIVTGIG
CSGNIPVPLK YNIVRALHGR ALAVATGIKL VRPDAEVVAF VGDGDLLSIG GNHFIHTIRR
NAGVKVILVN NMLYGMTGGQ VAPTTPMDAI THTTPYGNPE PPIDACRLAM ALGATYVARW
TVALSRQCIE SIKELLLHRG FGLLECLSQC PVYQGRYVIG IDRPSKIMDY HLKITVLGKE
PMYGDKITIG KFVDYEKPTY EEIIWSMINR VSKGGES
//
