ID A0A1H7EJD6_9BURK Unreviewed; 1186 AA.
AC A0A1H7EJD6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:SEK13197.1};
GN ORFNames=SAMN05518853_11272 {ECO:0000313|EMBL:SEK13197.1};
OS Variovorax sp. OK202.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1884311 {ECO:0000313|EMBL:SEK13197.1, ECO:0000313|Proteomes:UP000199192};
RN [1] {ECO:0000313|EMBL:SEK13197.1, ECO:0000313|Proteomes:UP000199192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK202 {ECO:0000313|EMBL:SEK13197.1,
RC ECO:0000313|Proteomes:UP000199192};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNZJ01000012; SEK13197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7EJD6; -.
DR Proteomes; UP000199192; Unassembled WGS sequence.
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; 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; 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 Pyruvate {ECO:0000313|EMBL:SEK13197.1}.
FT DOMAIN 484..630
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 759..946
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 973..1170
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1186 AA; 130285 MW; E0332BA062156C4B CRC64;
MNAPLPESVR KNLESASLDD KYSLDRGRAF MSGVQALVRL PMLQRQRDKA VGLNTGGFIS
GYRGSPLGSY DQALWSAQQH LKANHIVFQP GVNEELAATA LWGTQQLDLY PQSKQYDGVF
GIWYGKGPGV DRCADVFKHG NMAGTAKYGG VIAIAGDDHA AKSSTVAHQS DQLFMHCSMP
VFFPSSVQDI LDMGLHAFAL GRYAGVWTGM KTIQEVVESS ASVSVDPDRV KIILPEDVAL
PASGVHIRWP DTPLEQEARL FDTKWHAALA YMRANRLNHN VIEGPQDRFG IIASGKAYND
TRQALSDLGL DDATCRRLGI RLHKVNVVWP LEPSATREFA QGLQEILVVE EKREIMESQI
KELLYGWRDD VKPTVLGKYD PVAGLLADGM QANPADHWLL RAKADLTPAL IAKAIAKRLR
ALGLAPEGSE VAARMDARLA AVMHREQTLN NQTTETGERQ PWFCSGCPHN TSTRVPEGSR
AMAGIGCHHM VLTMDRSTST FSQMGGEGAA WVGQAPFTSD THVFSNLGDG TYFHSGLLAI
RQSIAAGVNI TYKILYNDAV AMTGGQRVGE RPEGHSVLQI QKSLLSEGIK KLVIVTDEPQ
KYEGVALESG VTVHHRDELD TIQREFRELL GTTAIIYDQT CATEKRRRRK RGKLATPAKT
VVINELVCEG CGDCSVQSNC LSVEPLETEF GRKRRINQNS CNKDFSCVKG FCPSFVTVEG
GTPKKQQKKQ RDPSVQLALP EPVLPSTEEP WSIIVAGVGG TGVITIGQLL GMAAQLEGKG
VVTQDAAGLA QKGGATWSHV QIANRPEAIL TTKIDVAKAD LVIACDAIVG ASKYTMSVMR
EGHTQVALNT HGTPTAAFVR NPQWSFPGEN CETVLAATVG AERVGGFDAE EVAVELVGDA
IYTNPLMLGY AWQKGHVPLS HAALMRALEL NGVQIENNKA AFEWGRRCAH DLRSVKALFQ
AASVIQFVRK PSLDEIVKQR VDFLTEYQNA AYAVAYSSFV EHVRATEAPL SSTRLSETVA
RYLFKLMAYK DEYEVARLHT DPAFTKRIAE MFEGDVKVVH HLAPPLLAKT NAKGELIKQA
YSGWIRWGFW LLRRMKGLRG TPFDPFGRTE ERKTERALIG EYKSCVEELI LGLTRDKLAL
AVEIAAIPEQ IRGYGHVKAR HLALARTQWD SLRGQWRDDG AKRRVA
//
