ID   A0A3S2UIR2_9BURK        Unreviewed;      1172 AA.
AC   A0A3S2UIR2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase family protein {ECO:0000313|EMBL:RVT88772.1};
GN   ORFNames=EOD73_07335 {ECO:0000313|EMBL:RVT88772.1};
OS   Inhella crocodyli.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Inhella.
OX   NCBI_TaxID=2499851 {ECO:0000313|EMBL:RVT88772.1, ECO:0000313|Proteomes:UP000288587};
RN   [1] {ECO:0000313|EMBL:RVT88772.1, ECO:0000313|Proteomes:UP000288587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP-18 {ECO:0000313|EMBL:RVT88772.1,
RC   ECO:0000313|Proteomes:UP000288587};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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:RVT88772.1}.
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DR   EMBL; SACM01000001; RVT88772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S2UIR2; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000288587; 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   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.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:RVT88772.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288587}.
FT   DOMAIN          732..923
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          956..1154
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
FT   COILED          969..1016
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1172 AA;  127607 MW;  402D9066439FE8EB CRC64;
     MSDALPLRSY QLSDNLAADS GAVFLTGTQA LVRLLIMQKR VDERAGLKTA GFVSGYRGSP
     LGMVDQQLWK AKKFLEKAQV EFLPAINEDL AATAVLGTQR VALDPQRRVE GVYAMWYGKG
     PGVDRSGDAL KHGNVYGSSS QGGVLVVAGD DHGCVSSSMP HQSDLAMQAW FMPVLHPGNV
     AEYLEFGLYG WALSRFSGNW VGFKAISEVV ESGMTVDLDA VPLDFEHPID FTPATNLHIR
     QTDLPSLDLE SRLAHKLAAV KAFSKLNSVD KHIVSSPAAT LGIVTVGKAH FDFMEVLRRL
     DLDPNALAAA GVRVYKVGLV YPLEPTRIEA FTQGLTDVLV IEEKAPVVER QIKEMLFHRP
     AFQRPRVVGK SDEHGAPLLS ELGELRPSRI MAVVAEWLAR LNPALDRRHL VVDFTAPCVL
     SNAADATRRL PYFCSGCPHN TSTKLPEGSR ALAGIGCHFM ANWMERSTSG LVQMGAEGVD
     WAAMSRFTDA PHVFQNLGDG TYYHSGYLAI RQAIAARTNI TYKILYNDAV AMTGGQPVDG
     QTSVPQIARQ VEAEGVKRLA IVSDEIEKYD AHRALFPPGT TFHDRGDMDA VQRELREVKG
     VSVLIYDQTC AAEKRRRRKK KEFPDPPRRI FINEQVCEGC GDCGQASNCL SVVPVETDFG
     RKRAIEQTSC NKDFSCVNGF CPSFVSVDGA VLKKKVGASF TPADVQRELA AIGEPPAWTW
     TGPFDLLVTG VGGTGVVTVG ALITMAAHLE RKQASVLDFM GFAQKGGSVL SFVRVAPTAD
     LLNQVRIDTQ QADVLLACDL VVGASQDALQ TVKPGRTVIL ANTHELPTAA FVRNPDASLH
     AGELLEKMKF AVGQNGAEGK LQTLDAQGIA QRLLGDTMPS NIVMLGACWQ AGLVPVSHAA
     LMRAIELNNV AVEANKTAFA LGRLAYAAPA AIGRLGGEQK VLLNLSSDKL DGNEGLIARR
     VRFLTQYQNA AYAERYQALV AQVRAAEARL GEAGKAERLS KAVARYLAKL MAIKDEYEVA
     RLYTDGQFEA SLKAQFERWD GLRFHLAPPL LAKPGSDGRV KKLTYGGWMW KAFGVLARFK
     GLRGTALDVF GHTAERRMER QLLADYEALV RELVAGLTPE KLELALQLAR LPERIRGYGH
     VKHANVTAVR QQWADMLARY RAAAPQPEAL TA
//