ID   T0ALH0_9RHOO            Unreviewed;      1180 AA.
AC   T0ALH0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:EPZ13689.1};
GN   ORFNames=M622_08300 {ECO:0000313|EMBL:EPZ13689.1};
OS   Thauera terpenica 58Eu.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=1348657 {ECO:0000313|EMBL:EPZ13689.1, ECO:0000313|Proteomes:UP000015455};
RN   [1] {ECO:0000313|EMBL:EPZ13689.1, ECO:0000313|Proteomes:UP000015455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=58Eu {ECO:0000313|EMBL:EPZ13689.1,
RC   ECO:0000313|Proteomes:UP000015455};
RA   Liu B., Frostegard A.H., Shapleigh J.P.;
RT   "Draft genome sequence of Thauera terpenica.";
RL   Submitted (JUN-2013) 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:EPZ13689.1}.
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DR   EMBL; ATJV01000125; EPZ13689.1; -; Genomic_DNA.
DR   RefSeq; WP_021251085.1; NZ_ATJV01000125.1.
DR   AlphaFoldDB; T0ALH0; -.
DR   STRING; 1348657.M622_08300; -.
DR   PATRIC; fig|1348657.5.peg.3703; -.
DR   eggNOG; COG1014; Bacteria.
DR   eggNOG; COG4231; Bacteria.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000015455; Unassembled WGS sequence.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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; -; 1.
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; IPR009014; Transketo_C/PFOR_II.
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   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015455}.
FT   DOMAIN          730..916
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          965..1163
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1180 AA;  128659 MW;  F495A9DD82119CEF CRC64;
     MSSGKNTVNA FTQEEGDIHL GGIDAIVRLT LDQVRTDARR GLTTGMFVSG YRGSPVGMLD
     AALIKQQKLL LQHHIHFVDG VNEDLAATAV WGTQMLHTVG KQKFDGVTGM WYGKAPGVDR
     SGDALKHANY TGIGKNGGVL AIAGDDPSCK SSSLCSQSEP MLYHVGIPSL YPGNVQEILD
     FGLHGYQMSR LAGLWAGMKI VTNVADGSGT ACVSPERLNF ITPDLSFDGE IFTPTMNMGM
     NVRAEALQME QSLYTRRLEV AKRYARANNL NNVVFSNPDA WIGIITAGKT YNDLNQAFLE
     MGLDDAALRH YGIRILKMGM LFPMEPTIVR EFAQGLEEIF VIEEKRPFLE MFAKQVLYGM
     SNAPRIVGKF DEEERELLPH YGELESDIIV RALLKRLSRK TRIESAENWL KRLDEIHSRN
     KLPTAVRTAW YCSGCPHNTS TTALDDSIVS AGIGCHTMAM WMGRNVVMGT HMGAEGTQWI
     GMAPFTEAQH IFQNMGDGTY AHSGSLAIRY AASTGVNITF KLLRNAHTSM TGGQAIQGEV
     PVVNMVAELL ANGVNKVIVT TDDPSRFNAV QLPGGTEVWH RDRLDEAQRV LAAIAGTTVL
     LHDQECAAEL RRARSRGKAD EPAEVIVINE RVCEGCGDCG EKSNCMSVEP VHTEFGRKTR
     IHQSSCNKDY SCVKGFCPSF LTITPHPAPA TDGAPRKKKG RIPALERALP APVKKVDDSL
     GFGIHVMGIG GTGSVTVVAT LAKAARLEGK HVIGLDQTGL AQKGGAVISD IKITHAPFKG
     SNKISDGRAD LYLGFDILNA TDPKNLDKCN PERTIAVVST TETPTGQMVA NRKVLFPASG
     GLTAGIDRVT RKSDNVFLDG QALAEGLFGD AMATNNFMVG VAFQAGTIPL QAESIEAAIR
     ESGVAVDMSL AAFRWGRMAV IDRGFVDAEI VRQHASGAVL TLHRAPQLSA VARNIVDSIG
     ADAEVRRLVE VRVPELIAFQ DEAYARRYAD AIKRVVATEQ RVFPGSALSE AAARYLYKLM
     AFKDEYEVAR LHTDPAFIAE LDAQFPHGYS VKYNLAPPLL AKTDPATGHL QKKQYGEWMF
     KAFKRMAGLK RFRGSALDVF GKTAERRMER QLIEDYLQLL EQIIAQLSPV NHGAAVALAS
     VPDEIRGYGH VKEKSLAVAR ELQATRLRAF LAPQQERQVA
//