ID T1XJW5_VARPD Unreviewed; 1200 AA.
AC T1XJW5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative indolepyruvate ferredoxin oxidoreductase, alpha/beta subunit {ECO:0000313|EMBL:AGU52574.1};
GN ORFNames=VAPA_2c00090 {ECO:0000313|EMBL:AGU52574.1};
OS Variovorax paradoxus B4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1246301 {ECO:0000313|EMBL:AGU52574.1, ECO:0000313|Proteomes:UP000016223};
RN [1] {ECO:0000313|EMBL:AGU52574.1, ECO:0000313|Proteomes:UP000016223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:AGU52574.1,
RC ECO:0000313|Proteomes:UP000016223};
RA Schuldes J., Brandt U., Hiessl S., Wuebbeler J.H., Thuermer A.,
RA Steinbuechel A., Daniel R.;
RT "Genome sequence of Variovorax paradoxus B4.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003912; AGU52574.1; -; Genomic_DNA.
DR RefSeq; WP_021003407.1; NC_022234.1.
DR AlphaFoldDB; T1XJW5; -.
DR KEGG; vpd:VAPA_2c00090; -.
DR PATRIC; fig|1246301.3.peg.5531; -.
DR HOGENOM; CLU_009166_1_0_4; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000016223; Chromosome 2.
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; 3.40.50.970; -; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:AGU52574.1}.
FT DOMAIN 752..938
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 969..1169
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1200 AA; 130894 MW; B5F063443781FFCF CRC64;
MNAPHKTTAL QRPGYQLSDN LWADAGAVFI TGTQALIRIL AMQKQRDAAR GLHTQGFVSG
YRGSPLGMVD QAIWKAGERF KETGIRFVPA VNEELAATQV LGTQRVESDP ERTVDGVYAM
WYGKGPGVDR AGDALKHGNA YGSSPHGGVL VVAGDDHGCV SSSMPHQSDH AFMAWRMPVM
QPASVAEYLE FGLYGYELSR YSGAWVGMAA LSEIVESAGT VDLDAVNVRV AAWEDADAVR
AATGHRPPAD GLHYRWPDLP SLRIESRLED KLAAVAAFTR RNSIDRHVIV SPHAKVGIVT
CGKAHHDLME VLRRLELTPA QLARAGVRLY KVGLSFPVEQ TRLKAFAQGL DEILVVEEKG
AVVETQLRDI FYNAPADARP VLVGKHDREG QPLVSALGEL RPSRLIELVA HWLAVHFPDN
HDLGDHLQHV RDFTPPELLG NASDAVKRLP YFCAGCPHNT STKVPEGSTA RAGIGCHFMA
NWMDRSTAGL IQMGGEGVDW ISHAMFTKTP HVFQNLGDGT YYHSGYLAIR QAVAAKATLT
YKILFNDAVA MTGGQPVDGV ISVDAIARQV ESEGVRQVVV VSDEISKYDD IKDRFPKGTE
FHDRAALDDV QRRLRELPGV TVLIYEQTCA AEKRRRRKKG ELADPPRRLY INEAVCEGCG
DCTVQSNCVA VLPHETPMGR KRKIDQTSCN KDYSCAKGFC PSFVGVTGGK LRRKSGALAA
GRDAFLHRVA ALAHPAPHAW TGPYDLLVTG VGGTGVVTVG AVIAMAAHLE GKSASVLDFM
GFAQKGGSVL SFVRLADAPE RLNQVRIDTQ QADAILACDV VVGASADALQ TVRHGRTRVL
ANIHEIPVAE SLRNPDAELH VDLLLEKMRF VAGEAQVETF DAQSLAEEFL GDTLAANIVA
TGYAWQRGLV PLSLEALMHA IELNGVAVAA NQSAFSLGRL AAGDPAALEQ LRAAPMQVQA
QQAEERPLDA LLADARRHLT GYQNAAWAQR FEKRVRMLQA AESALPGGDT RLPFTRNAAR
SLLKLMSYKD EYEVARLYTD GAFLQKLKDQ FEGDLQLEFH MAPPLLSRAG HGRTPAKIRL
GAWMLPVMKW LAHGKRLRGT KFDLFGYTQE RRTERAMIIQ FDHRLGELVA ELSPANQQLA
AQIAALPLSV RGFGHVKLAN LALATEREAE LLHRFAPQRY PRPEKNAQAG QFKGIAVVSQ
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