ID   A0A166RP99_9ACTN        Unreviewed;       662 AA.
AC   A0A166RP99;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:OAA26893.1};
DE            EC=1.2.7.3 {ECO:0000313|EMBL:OAA26893.1};
GN   ORFNames=UG55_101173 {ECO:0000313|EMBL:OAA26893.1};
OS   Frankia sp. EI5c.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA26893.1, ECO:0000313|Proteomes:UP000077018};
RN   [1] {ECO:0000313|EMBL:OAA26893.1, ECO:0000313|Proteomes:UP000077018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI5c {ECO:0000313|EMBL:OAA26893.1,
RC   ECO:0000313|Proteomes:UP000077018};
RX   PubMed=27389275;
RA   D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA   Tisa L.S.;
RT   "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT   Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT   Nodules of Elaeagnus angustifolia.";
RL   Genome Announc. 4:e00660-16(2016).
RN   [2] {ECO:0000313|EMBL:OAA26893.1, ECO:0000313|Proteomes:UP000077018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI5c {ECO:0000313|EMBL:OAA26893.1,
RC   ECO:0000313|Proteomes:UP000077018};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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:OAA26893.1}.
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DR   EMBL; LRTK01000011; OAA26893.1; -; Genomic_DNA.
DR   RefSeq; WP_066065512.1; NZ_LRTK01000011.1.
DR   AlphaFoldDB; A0A166RP99; -.
DR   STRING; 683316.UG55_101173; -.
DR   PATRIC; fig|683316.3.peg.1946; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000077018; Unassembled WGS sequence.
DR   GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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   ECO:0000313|EMBL:OAA26893.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077018}.
FT   DOMAIN          27..216
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          264..484
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
SQ   SEQUENCE   662 AA;  69444 MW;  F7640C498C56F63F CRC64;
     MTTELEQPDP RVRRLKGVVI RFAGDSGDGM QLTGDRFGAQ AAEAGNDVAT LPDFPAEIRA
     PAGTVGGVSS YQLHVADHDI TTPGDQPDVL VAMNPAALKA TLKDLRPGGV LLVDSGAFNV
     RSLEKAGYDS DPLTDGSLAN YIVHAVDLTG LAVGATEGLG LKRKDAARTK NMFALGLVSW
     MFNQPIESTI AYLEKRFAKK PPEILAGNLA ALRAGVDYGD TTEAFAVSYE VKPAALPPGQ
     YRHMRGNRAI AFGLVAAAHQ AGMPLFLGAY PITPATDVLH ELSKLISHDV RSYQAEDEIA
     AIGAAIGGSF AGMLGVTVTS GPGMALKSEA IGLAISLELP LVIVNVQRGG PSTGLPTKTE
     QSDLLQALYG RHGEAPLPVL AAQSPADCFN AAFEAAQIAL ERRTPVILLS DSYIANGSEP
     WKVPDVSELP DLGIEFATEP NGVGKDGQPA FHPYKRDPRT LARPLAIPGT PGLEHRIGGL
     EKADGSGEIS HDADNHDLMV RTRQNKVDGI EVPPLEVDDP SGPPGFGAKL LVIGWGSTYG
     PIGAACRLVR DQGLAIAQAH LRYLNPLPAN LASVLAAYDT VLVPEMNLGQ LGGLLRMHCQ
     VEPVGYTQTR GLPFRAVELA AVFTRLANDA EVGGAPLTTE DIKAIGGTGN VGRSELGSEG
     DK
//