ID X6Q0H1_9BACT Unreviewed; 632 AA.
AC X6Q0H1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:ETS98512.1};
GN ORFNames=HMPREF1505_1163 {ECO:0000313|EMBL:ETS98512.1};
OS Prevotella sp. ICM33.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1161412 {ECO:0000313|EMBL:ETS98512.1, ECO:0000313|Proteomes:UP000019890};
RN [1] {ECO:0000313|EMBL:ETS98512.1, ECO:0000313|Proteomes:UP000019890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICM33 {ECO:0000313|EMBL:ETS98512.1,
RC ECO:0000313|Proteomes:UP000019890};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-2014) 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:ETS98512.1}.
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DR EMBL; JACD01000054; ETS98512.1; -; Genomic_DNA.
DR RefSeq; WP_036923789.1; NZ_JACD01000054.1.
DR AlphaFoldDB; X6Q0H1; -.
DR PATRIC; fig|1161412.3.peg.1262; -.
DR Proteomes; UP000019890; 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 257..453
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 514..579
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 632 AA; 68954 MW; 48E93401CD25B293 CRC64;
MEEQIEVKEL DSVVVHFSGD SGDGMQLAGN IFTTVSATVG NGVSTFPDYP ADIRAPQGSL
TGVSGFQVHI GAGKVYTPGD LCDVLVAMNA AALKMQYKHC KPNSTIIIDT DSFGQRDLQK
AEFRSDDYLG EMGIDPDRVV ACPITKMVKD CLADTGMDNK SMLKCRNMFA LGLVCWLFNR
DLELVNNYLE TKFKKKPAIA EANIKVVRAG YDYGHNVHAS VPNTYRIEST VKQPGRYMDI
TGNKATAYGL MAAAERAGLR LFLGSYPITP ATDILHELSK HKSMGVTTVQ CEDEIAGCAS
AIGAAFAGAL AATSTSGPGI CLKSEAMNLA LIDELPLVII DVQRGGPSTG MPTKSEQTDL
LQVLYGRNGE SPMPVIAATS PTDCFDAAYN ACKIALEHMT PVVLLTDAFI ANGSSAWKLP
NIEDLPEIHP HFVTEDQKYK YTPYKRDPKT LARYWAIPGT EGYTHILGGL EKDGETGAIS
TDPENHDKMD HIRWNKVARI PVPDLTVLGD KDDADLLIVG FGSTYGHLYS AMEVLRGKGH
KVALAQFKYV NPLPKNTAEV LSRYKKVVVA EQNLGQLAAL LRIRINHFAP YQYNQVKGQP
FVVTELVTTF EKLLKAPLPK EETGTFYTKI LE
//
