ID A0A0G0NWL7_9BACT Unreviewed; 579 AA.
AC A0A0G0NWL7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:KKQ90254.1};
GN ORFNames=UT11_C0010G0016 {ECO:0000313|EMBL:KKQ90254.1};
OS Berkelbacteria bacterium GW2011_GWA2_38_9.
OC Bacteria; Candidatus Berkelbacteria.
OX NCBI_TaxID=1618334 {ECO:0000313|EMBL:KKQ90254.1, ECO:0000313|Proteomes:UP000033934};
RN [1] {ECO:0000313|EMBL:KKQ90254.1, ECO:0000313|Proteomes:UP000033934}
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:KKQ90254.1}.
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DR EMBL; LBVO01000010; KKQ90254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0NWL7; -.
DR PATRIC; fig|1618334.3.peg.205; -.
DR Proteomes; UP000033934; 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; 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; 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 Pyruvate {ECO:0000313|EMBL:KKQ90254.1}.
FT DOMAIN 12..174
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 212..451
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 579 AA; 63275 MW; 912E723C5CD1A966 CRC64;
MVDFQIKIAG AAGDGAMAVG LLASKALSRA GFYIFNYSEY PSLIRGGHNT TTVRASSEPV
GSISPKIEIM VALNSESFSM HEDELIDGGI LLWDQKESDH HVCKRGIHCI HVPFREISKS
LGNPLFLNTV ALGALSASLN FSLEFINAAL KSEFGRKGEA IVSANIKAAK AGFEFVRKNY
KAKLPADLAE FIEEKEDKDR VVMTGNEACA LGAIAAGCGF FAAYPMTPAS AILDEMSALS
AKTGILVKQT EDEISAINMT IGASFAGARV MTATSGGGFA LMCESLGLAA MTETPLVLIE
AMRPGPATGL PTWTDQGDLR FVLHAAQGEF PRIILSPGDA DEAIRLTHLA FDLADEYHIP
VIILTDKNLA ESSYSATWLT KSEQKFTRYG FISDTQLKHS KDYKRYKITA DGVSPRSIPG
QAGGIFRANS DEHTEYGFSS EEALNRSQMM EKRFRKTEHL SAHLPKPEVY GHSKPKITLF
GFGSTKWAIR EAVDILTSKK IKTRAVHLPV CWPLPTVSLS HYINSSERNF VIENNFTGQL
EGLIKQETGD VFDGHLRKYD GRPFLAEEVA EYARRKISN
//
