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Database: UniProt
Entry: E1KQS2_9BACT
LinkDB: E1KQS2_9BACT
Original site: E1KQS2_9BACT 
ID   E1KQS2_9BACT            Unreviewed;       632 AA.
AC   E1KQS2;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:EFL46127.1};
GN   ORFNames=HMPREF9296_1153 {ECO:0000313|EMBL:EFL46127.1};
OS   Prevotella disiens FB035-09AN.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=866771 {ECO:0000313|EMBL:EFL46127.1, ECO:0000313|Proteomes:UP000003610};
RN   [1] {ECO:0000313|EMBL:EFL46127.1, ECO:0000313|Proteomes:UP000003610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB035-09AN {ECO:0000313|EMBL:EFL46127.1,
RC   ECO:0000313|Proteomes:UP000003610};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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:EFL46127.1}.
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DR   EMBL; AEDO01000035; EFL46127.1; -; Genomic_DNA.
DR   RefSeq; WP_004356534.1; NZ_AEDO01000035.1.
DR   AlphaFoldDB; E1KQS2; -.
DR   STRING; 866771.HMPREF9296_1153; -.
DR   eggNOG; COG0674; Bacteria.
DR   eggNOG; COG1014; Bacteria.
DR   Proteomes; UP000003610; Unassembled WGS sequence.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR03710; OAFO_sf; 1.
DR   PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          22..212
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          261..444
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          514..585
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   632 AA;  68621 MW;  842C4349C92D7575 CRC64;
     MEEQIEVKEL EHVVVLFSGD SGDGMQLAGN IFSNVSATVG NGISTFPDYP ADIRAPQGSL
     TGVSGFRVHI GAGKVYTPGD KCDVLVAMNA AALKTQYKNC KPQGTIIIDT DSFSARDLKK
     AEFQTDDYLK EMGIDSDRVV ACPITKMVKD CLADTGMDNK AMLKSRNMFA LGLVCWLFNR
     DLELVNNFLN DKFKKKPAVA EANIKVVAAG YNYGHNVHAS VPNTYRIETK EKVAGRYMDI
     TGNKATAYGL MAAAEKAGLT LFLGSYPITP ATDILHELAK HKSMGVVTVQ CEDEIAGAAS
     AIGAAFAGAL SATTTSGPGI CLKSEALNLA VIDELPLVIV DVQRGGPSTG LPTKSEQTDL
     LQVLYGRNGE SPMPVIAATS PTDCFDAAFQ ACKIALEHMT PVVLLTDAFI ANGSSAWKIP
     SMDKLPTIKP HFAPESQKFK YTPYKREDYT NVRYWAVPGM EGFEHILGGL EKDGKTGAIS
     TDAENHNLMD HLRFDKVARI PVPDLEVQGD ADDADLLIVG FGSTYGHLYS AMQELRAKGH
     KIALAQFKYV NPLPKNTAEV LAKYKKVVVA EQNLGQLAAL LRIRINNFAP YQYNQVKGQP
     FVVQELVQGF ERLLTLPAPK DESGMFYSRI LQ
//
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