ID D6CP49_THIA3 Unreviewed; 1208 AA.
AC D6CP49;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:CAZ90327.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:CAZ90327.1};
GN OrderedLocusNames=THI_3752 {ECO:0000313|EMBL:CAZ90327.1};
OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ90327.1, ECO:0000313|Proteomes:UP000002372};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3As;
RA Genoscope - CEA;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22701 / CIP 110005 / 3As
RC {ECO:0000313|Proteomes:UP000002372};
RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT "Structure, function, and evolution of the Thiomonas spp. genome.";
RL PLoS Genet. 6:E1000859-E1000859(2010).
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DR EMBL; FP475956; CAZ90327.1; -; Genomic_DNA.
DR RefSeq; WP_013107536.1; NZ_CTRL01000001.1.
DR AlphaFoldDB; D6CP49; -.
DR KEGG; thi:THI_3752; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_009166_1_0_4; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000002372; Chromosome.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
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 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 ECO:0000313|EMBL:CAZ90327.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002372}.
FT DOMAIN 486..635
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 767..954
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 981..1182
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
FT REGION 723..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 132044 MW; F66E11257C1282DA CRC64;
MNAPLPEHIR RALATISLDD KYTLDSGRAF MSGIQALVRL PMLQRQRDAA VGLNTAGFVS
GYRGSPLGGY DQALWKAKKI LEANHVVFKP GVNEELAATA VWGTQQLDLF PDKNKFDGVF
GIWYGKGPGV DRCSDVFKHA NSAGTARHGG VIAVAGDDHV AKSSTLAHQS DHIFKACGLP
VFFPTSVQDI LDLGVHAFAL SRYAGVWSGM KTIQEIVESS ATVDVDADRV RILLPEDFAL
PPDGVHIRIP DTPLAQEARL MDVKWYAALA YIRANRLNHT VIDSPHARLG IMASGKAYND
TRQALNDLGL DADTCAQLGI RLHKVAVVWP LEAQLTREFA TGLQEILVVE EKRQVIEYQL
KEELYNWRED VRPNVIGKFD EIAGDRTGGE WSQPNPGGNW LLPAKADLNP AIIARAIAAR
LERLGILRDA GVDVQRRISE RLAVIDARER TLQAPGASAQ RPPWFCSGCP HNTSTRVPEG
SRGMAGIGCH YMVVWMDRAT QTFSQMGGEG VAWVGQAPFT TDEHVFVNLG DGTYYHSGLL
AIRQAISAGV NATYKILFND AVAMTGGQPV EGGLTVPQIS RELEAEGVRR IVVVTDEPQK
YDNAVGLASG ATVRHRDDLD AIQRELREEA GITVIIYDQT CATEKRRRRK RGLMVDPARR
VVINPLVCEG CGDCSDQSNC LSVEPLETEF GRKRTINQSS CNKDFSCLKG FCPSFVTVEG
GALRKPKPQP GADLSSMPEL PQPEVPDPVR DDVAGGGSYG IVVAGVGGTG VITIGQLLGM
AAHIEGKGVV TQDAAGLAQK GGATWSHVLI ANDPQQIVTT RVGTAEAELI LGCDPIVTAD
RETLARVREG RTHIALDTHS TPTAAFVHNP DWQFPDAACH KTIEQAAGTD HVAGFDCVRA
AEKLLGDAIY ANPMLLGFAW QKGWVPLSHA ALMRAIELNA VQVEKNKAAF EWGRHAAHDP
QGIAALSAAE QVIQLVKRPS LDEIIQRRVE FLTGYQNAAY ARQYADFVSQ VRAAEAPLKS
TALTEAVARH LFKLMAYKDE YEVARLQSDP AFAKQLQEQF EGHFKRHYYL APPLWSKRNA
KGELIKREFG PWMGVAFRLL APLKVLRGTA LDPFGHTAER KQERALIGQY RETIAELLRG
LNANSPPERL QLATQIARLP DGIRGYGHIK QRYLAQVLPQ WEALMRKWRQ VTAGASSPDS
QAVPETVA
//
