ID   A0A0N7J9D8_9BURK        Unreviewed;      1184 AA.
AC   A0A0N7J9D8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:ALK90712.1};
GN   ORFNames=L103DPR2_00298 {ECO:0000313|EMBL:ALK90712.1};
OS   Limnohabitans sp. 103DPR2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1678129 {ECO:0000313|EMBL:ALK90712.1, ECO:0000313|Proteomes:UP000063254};
RN   [1] {ECO:0000313|EMBL:ALK90712.1, ECO:0000313|Proteomes:UP000063254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103DPR2 {ECO:0000313|EMBL:ALK90712.1,
RC   ECO:0000313|Proteomes:UP000063254};
RA   Ahn J.-H., Kim S.B.;
RT   "Limnohabitans sp. 2 strains.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP011834; ALK90712.1; -; Genomic_DNA.
DR   RefSeq; WP_055359435.1; NZ_CP011834.1.
DR   AlphaFoldDB; A0A0N7J9D8; -.
DR   STRING; 1678129.L103DPR2_00298; -.
DR   KEGG; lim:L103DPR2_00298; -.
DR   PATRIC; fig|1678129.3.peg.289; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000063254; Chromosome.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02008; TPP_IOR_alpha; 1.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR046667; DUF6537.
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; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF20169; DUF6537; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063254}.
FT   DOMAIN          485..635
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          763..950
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          977..1174
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1184 AA;  130323 MW;  C1585D49B91B5F6B CRC64;
     MNAPLPEHLR QALANVTLDD KYSLATGRAF MSGVQALVRL PMLQQERDAL ADKKTGALIS
     GYRGSPLGGY DQALWKAKPY LEKHNIVFQP GVNEELAATA LWGTQQLGFA PPGSNKMDGV
     FGIWYGKGPG VDRCSDVFKH ANMAGTTPWG GVLAVAGDDH VAKSSTAAHQ SDHIFKACGL
     PVFFPASVQE VLDLGVHAIG LSRFAGVWSG MKTIQEIVES SATADINADR VKIVLPDFEM
     PPGGVHIRWP DSALEQEARL FDFKWYAALA YIRANRLNHN VIEGPQDQYG IIASGKAYND
     TRQALVDLGL DNETCQRLGI RVHKVSVVWP LEAQTTREFA QGLKEILVVE EKRQIIEYQL
     KEELYNWPDS KRPRIVGKFD ELDGDDAGGE WSVPNPMAHR LLRANADLTP TLIAKALAHR
     LLKLDLPSDI VARMNAQLQI IESKERSQNS LVLNPAADRM PWFCSGCPHN TSTKVPEGSR
     AMAGIGCHFM SLWMDRSTVG FTQMGGEGTP WIGQQHFSNE QHVFANIGDG TYFHSGILAI
     RQSIAAGVNI TYKILYNDAV AMTGGQRVGE RAEGHSVVQI AQSMRAEGAV VIKVVTDEPE
     KYNGVALAEG VLVHHRDELD AIQRELREVK GCTVIIYDQT CATEKRRRRK RGTMVDPAVR
     VMINELVCEG CGDCGVQSNC LSVEPLETDF GRKRTINQNT CNKDTSCLKG FCPSFISIEG
     GQLRKKSKEQ KFSPAQLPAL NLPRLPDLSS SFNAYGIVVA GVGGTGVITI GQLLGMAAHL
     DGLGIVTQDS AGLAQKGGST WSHVLLAKHQ DHIQTTRVSM AAADLILGCD PIVSAGKETL
     SRMRQGRTHV ALNSHSTPTA AFVKDTQWVN PAESCAQEIA NAVGLEGLAA FDADKLSAQL
     MGDTIYINPM ILGYAWQKGW VPLSLEALQR AIELNEVAVA NNLAAFEWGR HAAQHLEAVE
     ALLTPAQVIQ FKKRDRLEDL IAQRVEFLTA YQNTAYAKQY ENFVGLVKQK EQALGQSLLT
     ETVARQLFKL MAYKDEYEVA RLHTDKQFLE RVKTQFEGDF KVFYHLAPPL IAKRNEKGHL
     IKQKMSPSTL LVFKALAHFK FLRGTAFDIF GKTEERQTER ALIQEYKDAV SEVIASLKAD
     NHALAVQVAK VPEQIKGFGH VKERNLSAAM VQWQNSMDAF RKSI
//