ID A0A2V3PNW8_9BACT Unreviewed; 614 AA.
AC A0A2V3PNW8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:PXV64370.1};
GN ORFNames=CLV62_11013 {ECO:0000313|EMBL:PXV64370.1};
OS Dysgonomonas alginatilytica.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=1605892 {ECO:0000313|EMBL:PXV64370.1, ECO:0000313|Proteomes:UP000247973};
RN [1] {ECO:0000313|EMBL:PXV64370.1, ECO:0000313|Proteomes:UP000247973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100214 {ECO:0000313|EMBL:PXV64370.1,
RC ECO:0000313|Proteomes:UP000247973};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PXV64370.1}.
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DR EMBL; QICL01000010; PXV64370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3PNW8; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000247973; 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; 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..211
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 260..434
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 614 AA; 67005 MW; DFBDF40382489688 CRC64;
MLEKIQVNDV QDIVIRFSGD SGDGMQLSGT LFSNLSAILG NQISTFPDFP AEIRAPQGTL
SGVSGFQMHI GTQVYNSGDK ADVLVAMNPA ALKVNANQLK TNSIILVDTD SFQKRDLEKA
LFKTEDPFLE LGLTTQQIVA IPITTLTKDS LAAFELDMKS KIRCKNMFAL GVVCWLFNRP
IDIVNEMLST KFSKKPVLAD ANLQVLANGY NYGHNTSLSV SSYRVDTLQM DKGYYMDVNG
NSATAFGLIA AAEKANLQLF LGSYPITPAT DILHELVKRK DLGVKVVQAE DEIAGICIAI
GASFAGSLAV TSTSGPGLAL KGEAIGLAVM AELPLVIVDV QRGGPSTGLP TKTEQTDLRQ
ALYGRNGESP IVVIAGSSPT NCFDTAYWAS KIALEHITPV ILLTDSYIAN GSSSWKIPNM
EEYPSIKPND ISLYTGDEWT VAARNEDNYA RYWAPAGTEG YTHRIGGLER DYFTGAISTD
PDNHQKMVDT RQAKIDRIAD FIPELEVLGD TDSKTLVVGW GGTYGHLREA VEEMSKGENK
VALAHFNFIS PLPRNTESVL RKYDKIIVAE QNNGQFAGYL SEKFNNLPMI KYNKVNGQPF
VVSDLIDFFT QEIK
//
