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Entry: A0A1I7N8K0_9BACT
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ID   A0A1I7N8K0_9BACT        Unreviewed;       617 AA.
AC   A0A1I7N8K0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:SFV30913.1};
GN   ORFNames=SAMN05660895_0927 {ECO:0000313|EMBL:SFV30913.1};
OS   Thermoflavifilum thermophilum.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Thermoflavifilum.
OX   NCBI_TaxID=1393122 {ECO:0000313|EMBL:SFV30913.1, ECO:0000313|Proteomes:UP000199537};
RN   [1] {ECO:0000313|Proteomes:UP000199537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14807 {ECO:0000313|Proteomes:UP000199537};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FPCJ01000001; SFV30913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7N8K0; -.
DR   STRING; 1393122.SAMN05660895_0927; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000199537; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199537}.
FT   DOMAIN          22..213
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          262..473
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          518..586
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   617 AA;  67590 MW;  43AE86D48B379358 CRC64;
     MSTQTTVQQL RDVVIKFAGD SGDGMQLTGM QFTNNTALLG IDLSTFPDFP AEIRAPQGTL
     PGVSGFQLHF SSDPVYTPGD SCDVLVAMNA AALKANLKSL KKGGIIIANT DGFDAKNLRL
     ANYPEGVNPL TDGSLDGYIV YEIDITKLTR EALKDVDLGM KEKDRAKNMF VLGFLYWLYD
     RKMESTIHFL QEKFAKKPLI LEGNLKALHA GYNYGDTTEA FTTRYRVERA KMPRGTYRSI
     TGNQALALGL IAASQKSGLP LFLGSYPITP ASDILHELSK HKNFGVRTFQ AEDEIAGISS
     AIGASYGGCM GVTTTSGPGM ALKTEAMGLA VMLEIPLLII DIQRGGPSTG LPTKTEQSDL
     LQAYYGRNGE CPMPVIAAAT PSDCFSAVYE AFRIAVQYMT PVIFLSDGYI ANGAEPWRFP
     KAADLPPIEV KFKTQLDEGE EKFMPYQRDE RYVRPWAVPG TPGLEHRIGG LEKQHITGNV
     SYDPDNHQLM VKLRQAKVDA VADDIPLQTL DSGPESGDLL VLGWGSTYGA IKGAVKSLQQ
     QGYAVAHAHL RYLRPFPKNL GEILRNYKQV LIPEINNGQL IKIIRDQFLI DAKGYHKIMG
     IPITKSELEE HIKSLLG
//
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