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Database: UniProt
Entry: A0A0F2LA46_9CREN
LinkDB: A0A0F2LA46_9CREN
Original site: A0A0F2LA46_9CREN 
ID   A0A0F2LA46_9CREN        Unreviewed;       299 AA.
AC   A0A0F2LA46;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE            EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
DE   Flags: Fragment;
GN   ORFNames=TU36_01210 {ECO:0000313|EMBL:KJR72581.1};
OS   Vulcanisaeta sp. AZ3.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Vulcanisaeta.
OX   NCBI_TaxID=1609231 {ECO:0000313|EMBL:KJR72581.1, ECO:0000313|Proteomes:UP000054362};
RN   [1] {ECO:0000313|EMBL:KJR72581.1, ECO:0000313|Proteomes:UP000054362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Servin-Garciduenas L.E., Martinez-Romero E.;
RT   "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT   Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL   Submitted (MAR-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   -!- 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:KJR72581.1}.
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DR   EMBL; JZWU01000018; KJR72581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2LA46; -.
DR   Proteomes; UP000054362; 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: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:KJR72581.1}.
FT   DOMAIN          2..224
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          248..294
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   NON_TER         299
FT                   /evidence="ECO:0000313|EMBL:KJR72581.1"
SQ   SEQUENCE   299 AA;  33322 MW;  88C1CF83A7E82632 CRC64;
     MARVNVISAY PITPQTLIVE RISEMIDKGE LKADYIRVES EFAALATVYG AASAGARAFT
     ATSSHGLFYM YEMLWWAAAS RIPFVMAVVT RVVGPPWNIH NEHTDLLAIR DSGWIIGMAQ
     NVQEAFDMTL TAFKISEDER VLLPVAVGLD GFVLSHTAEP LYIPSQDDVD AWLPPRNPRI
     PYVIEPGGES ITMGNLPKDD VYHALLKKYM DESMESAKKV IAEVYDEYGK LTGRNYGPLT
     ECYMCGDAKY IAVSMGAWSG DILTAIERLR DEGYPVGLLR LRYVRPFPEE DIIAWINGA
//
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