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
//