ID A0A0G0M507_9BACT Unreviewed; 588 AA.
AC A0A0G0M507;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein, 2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KKQ68734.1};
DE EC=1.2.7.3 {ECO:0000313|EMBL:KKQ68734.1};
GN ORFNames=US89_C0006G0075 {ECO:0000313|EMBL:KKQ68734.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_38_29.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619066 {ECO:0000313|EMBL:KKQ68734.1, ECO:0000313|Proteomes:UP000033957};
RN [1] {ECO:0000313|EMBL:KKQ68734.1, ECO:0000313|Proteomes:UP000033957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ68734.1}.
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DR EMBL; LBUS01000006; KKQ68734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0M507; -.
DR STRING; 1619066.US89_C0006G0075; -.
DR PATRIC; fig|1619066.4.peg.581; -.
DR Proteomes; UP000033957; Unassembled WGS sequence.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:KKQ68734.1}; Pyruvate {ECO:0000313|EMBL:KKQ68734.1}.
FT DOMAIN 14..177
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 212..452
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 476..548
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 588 AA; 64482 MW; CBCB1E44388EF091 CRC64;
MITNNLSWLI GGEAGQGLES AGHMFALVLN RGGLFVITNA EYPSLIRGGH NYNKVRVSDK
PLTCHTNDVD LVCALNKETF EKHIDEISNG GGIIYDSADF PDAKGKDGVN LFGIPMAELA
KTKGGGIIMK NVVAIGACIG LLDYDLNYFK EALKQTFGRK GDEIVNSNYN AAQAGYDYMQ
ENYKGKFGYN LAAMKDAKQR MLIQGNDAFC IGAIKGGCKL VAEYPMTPSS SILHFMAEHS
REYNVVVKHV EDEISAINTI IGASAVGIRS LTATSGGGFS LMVEAVGLAG MIETGIVIVN
VQRPGPSTGL PTRTGHPDLR LMMHASQDES PRMVVAPGDP EECFDLGFQA FNVADKYQIP
VMFLSDKYLS ESERSVDFFD TKELEIDRGK LLLEKDLDPK EDRYPRYKDS PDGISARPLA
GEKGGIFTCT SDEHNDYGDI VEDIPNRLEK MNKRMRKIDT LRKGLPAPKL IGPANADITF
VSWGSPKGSI LEAIELLAKD DVSANFLQIK YFIPFHSEEV AKILGKAKRI VDVEENFSGQ
LADLIREKTG IFIEERILDY SGRPFTAKQI YNEVKLKTGQ ASSKTVPV
//
