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Database: UniProt
Entry: A0A238YP68_9FLAO
LinkDB: A0A238YP68_9FLAO
Original site: A0A238YP68_9FLAO 
ID   A0A238YP68_9FLAO        Unreviewed;       618 AA.
AC   A0A238YP68;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:SNR72927.1};
GN   ORFNames=SAMN04488111_2703 {ECO:0000313|EMBL:SNR72927.1};
OS   Lutibacter flavus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=691689 {ECO:0000313|EMBL:SNR72927.1, ECO:0000313|Proteomes:UP000198412};
RN   [1] {ECO:0000313|Proteomes:UP000198412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27993 {ECO:0000313|Proteomes:UP000198412};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZNX01000005; SNR72927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238YP68; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000198412; 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}.
FT   DOMAIN          25..214
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          264..474
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
SQ   SEQUENCE   618 AA;  67909 MW;  E5E6E96889E7D258 CRC64;
     MISDKVKLQP EVIEAVVIRF VGDSGDGMQL TGTQFSDTSA MFGNDIATFP NYPSEIRAPQ
     GSLYGVSGFQ VHIGSVEVST PGDNLDLLVA MNPAGLKTNL YAVKPGHTII VDTDAFSKKN
     LEKAQYETNP LEDGSLENYR IIQVDMTSLT KEALKEVEGL DNKSIVRSKN MFALGMVYWM
     YGRSKEHTIE FFNKKFKTKP NLIEANTKVL NAGYFFAETL ELIPNAYTIS PAKMKPGTYR
     IIMGNTATAW GFLAAAEKSG LELFLGSYPI TPATDILHEL VKHKHFGVKA FQAEDEIAGI
     ASAIGASFAG DLAITTTSGP GLALKGEALG LAMIMELPLV VVNVQRGGPS TGLPTKTEQS
     DLLQAMYGRN GESPVIVIAA STPADCFQYA YEAAKLSLEH MTPVILLTDG YIANGSAPWK
     IKSLKDLPEI KNRISKNASE DFHPYERDEE TLARNWAIPG TAGLEHRIGG LEKDRITGNV
     SQAPENHEKM TKIRAEKIKR VQNFIPDIKT EFAETGDLLV IGWGGTYGSL HSAVKQINED
     GYKNIGFAHF NYINPLPKNT EELLTRFKKI IVCELNNGQF AKILRINFEG FKIHQFNKIQ
     GLPFGNNELI AEFKKLVD
//
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