ID A0A101XLE8_9CREN Unreviewed; 415 AA.
AC A0A101XLE8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=AT717_05095 {ECO:0000313|EMBL:KUO93489.1};
OS Vulcanisaeta sp. CIS_19.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=1714251 {ECO:0000313|EMBL:KUO93489.1, ECO:0000313|Proteomes:UP000054677};
RN [1] {ECO:0000313|EMBL:KUO93489.1, ECO:0000313|Proteomes:UP000054677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA Inskeep W.P.;
RT "The distribution, diversity and function of predominant Thermoproteales in
RT high-temperature environments of Yellowstone National Park.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO93489.1}.
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DR EMBL; LOCG01000103; KUO93489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101XLE8; -.
DR Proteomes; UP000054677; Unassembled WGS sequence.
DR GO; GO:0018491; F:2-oxobutyrate 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:KUO93489.1}.
FT DOMAIN 34..257
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 282..387
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 415 AA; 46184 MW; 8CCD98B92C92994F CRC64;
MAVSAIEAKR LEAVLKGDEE VEVVGTGTDA VAYALMLADI DVTAAYPIRP YGGVMERTAR
LIADGYLKAE YIVAAHEHDQ FEIVKHASAV GARAFVGSSG VGWLLAIEAI VAISTDRYPV
VALIGNRALD DPGAYGVEHN DALMVRDVGW LLVWVDTAQE ALDTTLIAYR IAEDPRVMLP
VGISMDGAFL THSEHVFRIP PKSKVQKFLP PYDLGNRKLH PSNVISVAPQ VNEDWVTELR
KQMDEAMKNA RRVIEEAYRD YAKIIGRDYG NPFVEPYMVD DADVIMVGMG TVSKPIKEAV
RRLRAKGERV GFLRIRWFRP FPTDDIIRYL TGAKAVAVVD RDYSFGSPFD GGALYTEIRS
ALYEAEHRPL MINFIGGLGG REITYNDAMN MFNITLDAAR KSKVEQRVIW YGVRE
//
