ID   A0A0Q8P0I7_9ACTN        Unreviewed;       648 AA.
AC   A0A0Q8P0I7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KRB67218.1};
GN   ORFNames=ASE03_02330 {ECO:0000313|EMBL:KRB67218.1};
OS   Kitasatospora sp. Root187.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB67218.1, ECO:0000313|Proteomes:UP000051829};
RN   [1] {ECO:0000313|EMBL:KRB67218.1, ECO:0000313|Proteomes:UP000051829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root187 {ECO:0000313|EMBL:KRB67218.1,
RC   ECO:0000313|Proteomes:UP000051829};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB67218.1, ECO:0000313|Proteomes:UP000051829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root187 {ECO:0000313|EMBL:KRB67218.1,
RC   ECO:0000313|Proteomes:UP000051829};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRB67218.1}.
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DR   EMBL; LMHX01000023; KRB67218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8P0I7; -.
DR   STRING; 1736486.ASE03_02330; -.
DR   Proteomes; UP000051829; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:UP000051829}.
FT   DOMAIN          52..239
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          288..502
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          543..607
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   648 AA;  69013 MW;  5F58C3AC093D8291 CRC64;
     MTSQVDQVEA VDGSDDGEGR SGPVPPPGVR QRPAKPIRRV DRVIIRFAGD SGDGMQLTGD
     RFTSETASFG NDLSTLPNFP AEIRAPAGTL PGVSSFQLHF ADHDILTPGD APNVLVAMNP
     AALKANLADL PRGAEIIANT DEFTKRALAK VGYAADPLGD GSLEAYHVHR VPLTALTLEA
     LKDSGLARKD AERAKNMFAL GLLSWMYHRP THGTEAFLRQ KFAKKPEIAE ANIVAFRAGW
     NFGETTEDFA VSYEVAPARL PLGTYRNISG NLALSYGLIA AGQRSGLPVF LGSYPITPAS
     DILHELSRHK NFGIRTFQAE DEIAGIGAAL GAAFGGALGV TTTSGPGVAL KSETIGLAVS
     LELPLLVVDI QRGGPSTGLP TKTEQADLLQ AMFGRNGEAP VPIVAPATPA DCFDAALEAA
     RIAVTYRTPV FLLSDGYLAN GSEPWRIPQV DELPLIDPDF ATGPNHDGEF WPYQRDPATL
     ARPWAVPGTA GLEHRIGGIE KQDGTGNISY DPANHDFMVR TRQAKIDGID VPDLEVDDPS
     GSARVLVLGW GSTYGPITAA VRRVRADGGE VAQTHLRHLN PFPANLGSIL KAYDKVIVPE
     MNLGQLALLL RAKYLVDAES YNQVRGLPFK AAQLADVLSA AIGTLEEK
//