ID I3UED5_ADVKW Unreviewed; 1186 AA.
AC I3UED5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:AFK63373.1};
GN OrderedLocusNames=TKWG_17340 {ECO:0000313|EMBL:AFK63373.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK63373.1, ECO:0000313|Proteomes:UP000005267};
RN [1] {ECO:0000313|EMBL:AFK63373.1, ECO:0000313|Proteomes:UP000005267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17095 / LMG 22695 / WT001
RC {ECO:0000313|Proteomes:UP000005267};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(2011).
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DR EMBL; CP003555; AFK63373.1; -; Genomic_DNA.
DR RefSeq; WP_014751464.1; NC_017964.1.
DR AlphaFoldDB; I3UED5; -.
DR STRING; 1036672.TKWG_17340; -.
DR KEGG; aka:TKWG_17340; -.
DR HOGENOM; CLU_009166_1_0_4; -.
DR OMA; FEWGRYL; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000005267; 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; -; 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; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR PANTHER; PTHR48084:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 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}.
FT DOMAIN 750..936
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 969..1170
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1186 AA; 131175 MW; 057267213905CEDB CRC64;
MNAPLPKVAQ DALKNTTIDD KYSLERGRVY MSGTQALVRL PMLQKDRDRR AGLDTGGFIS
GYRGSPLGNL DLSLWKAKKY LAEHEISFQP GVNEELGATA VWGSQQVNLF PGATKQGVFA
MWYGKGPGLD RSMDVFKHAN SAGSSQFGGV LLLAGDDHAA KSSTVAYQSE HNLQSAGIPV
LYPSNVQEYL DFGVHGWAMS RYSGLWVAMK CVTDVIESSS SVELDPDRVQ TITPPDFDMP
EGGLSIRWPD PPLDQEARLN NYKFYAALAY VRANKLDKII FDSPKARFGI MTAGKAYLDV
RQALTDLGLD EATCADIGIR LYKVGCVWPL EAQGARHFAE GLDEILVVEE KRQIMEYALK
EELYNWRDDV RPDVYGKFDA RDDGGGEWSV PRGNWLLPAN YELSPAIIAK AIAKRLEKHA
LPDEVRARIQ ARIAIIHAKE QDAKRPVVVQ DRKPWFCSGC PHNTSTRVPE GSRAVAGIGC
HYMTIWMDRS TDTFTQMGGE GVPWIGQKDF TTTKHIFANL GDGTYFHSGI LAIRASIAAK
VNITYKILYN DAVAMTGGQP VDGTLTVPQI NAQLHAEGAT RIVIVSDEPE KYKGVSLIGN
PDVFHRDSLD DVQLELRDTE GTTILIYDQT CATEKRRRRK RNAYPDPDRR VFINEAVCEG
CGDCGVKSNC LSVEPVDTPM GSKRRINQSS CNKDYSCLNG FCPSFVTAEG AKVRKPQTAT
LSFEKIEADI PEPATPVIDR SYNILVPGVG GTGVVTIGAL LGMAAHLEEK GVNVLDITGL
AQKGGAVVSH VQIGNQPADL HSTRIGVGEA DLIIGCDAIV AASREITSKT RKGITVAAIN
SAKVPTAEIF QNPKWQFPSA ITENDMLDLL GQEKCDFLDA NGYAVALLGD AIFANPLMMG
YAWQKGWIPL HHESLERAIE LNGVAVDKNL AAFEWGRYLA HHGLQSVPLG SSKRTARHEN
LISMPESTDT LIKRLAQHLT KYQNERYARR FTQAVARIRE TEKTRGFSGH ILTEAVARNL
AKLMSYKDEY EVARLYTDPA YFDKLREQFE GEPGRDYALH VHLAPPAFSK KDKKGHLIKK
KYGPWVMKAF AVLAHLKPLR GTALDPFGRT EERRAERALV EEYFALLDEI NQSLNDSNYD
TAVELARLPD DIRGYGHIKE ANMQKAAARR VQLLEDYRRT ALSKAA
//