ID Q8PE13_XANCP Unreviewed; 1190 AA.
AC Q8PE13;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase chain alpha {ECO:0000313|EMBL:AAM39489.1};
GN Name=iorA {ECO:0000313|EMBL:AAM39489.1};
GN Synonyms=AF1489 {ECO:0000313|EMBL:AAM39489.1};
GN OrderedLocusNames=XCC0170 {ECO:0000313|EMBL:AAM39489.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM39489.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM39489.1, ECO:0000313|Proteomes:UP000001010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC {ECO:0000313|Proteomes:UP000001010};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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DR EMBL; AE008922; AAM39489.1; -; Genomic_DNA.
DR RefSeq; NP_635565.2; NC_003902.1.
DR AlphaFoldDB; Q8PE13; -.
DR STRING; 190485.XCC0170; -.
DR EnsemblBacteria; AAM39489; AAM39489; XCC0170.
DR KEGG; xcc:XCC0170; -.
DR PATRIC; fig|190485.4.peg.193; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_009166_1_0_6; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000001010; Chromosome.
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 InterPro; IPR009014; Transketo_C/PFOR_II.
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.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001010}.
FT DOMAIN 706..892
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 973..1172
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
FT REGION 916..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 129131 MW; 0ACDE053C1858B6B CRC64;
MRLPLMQHLR DVAAGLDTAG FVSGYRGSPL GGLDLELWRA RAHLEAAKVT FTPGLNEDLA
ATMVWGTQQT NLFPGATVQG VYGMWYGKGP GVDRSGDVFK HANAAGTSPF GGVLALAADD
HACRSSTLPH GSEDEFVSAM MPILNPAGVQ DILDMGLLGW AMSRYTGRWV GFKTIAETVE
SSASVDVDPF ARQIVLPDDF ALPPGGLSIR WPDPPVDQEM RLHRYAVAAA QAFARANGID
KLVLDSPQAR LGIVTTGKSY LDVLQALEYL GLDAQACAQI GIRVYKVGMT WPLEPVGITA
FARGLDDIVV VEEKKAFIER QMKELFYNWP ASAGARPSIV GKYNEHGAWI LPSTGELTPA
TIAAVIGKRI QRFPLPSAAI AASIEQRLRW MEAKEAEMAL PRALFPRVPH YCSGCPHNTS
TVVPEGSRAL GGIGCHYMVT WMNRSTDTFT HMGGEGVTWS GQAPFTATPH VFQNLGDGTY
FHSGSLAIRQ SVATGVNITY KILYNDAVAM TGGQPVDGTL TVPDIAHQLR AEGIHEIVVV
SDDIGKWTRR RERFPSDVAF HDRSELDAVQ QRLRTIKGVS ILIFDQTCAT EKRRRRKRGK
LIDPPKRVMI NSLVCEGCGD CGEKSFCVSV LPKDTEFGRK REIDQSNCNK DYSCVSGFCP
SFVTVHGGAP RKGKKRDASA LLDALPEPPQ RTTLEQPWNI LITGVGGTGV VTIGALLGMA
GHLEGKGATV LDQTGLAQKG GAVTTHIRIA RQPADIHAVR IAAGEADLVL GCDMVVVNDY
WALSKVRDGR TQVVLNTYEA MPGSFTTQPD LQFPAAEIIA GVRTALGGQE PLLLDATQLA
TALLGDAIAS NLFVLGYAWQ HGLVPLSHAA LMRAIELNGA AVAMNQQAFA WGRLAAVDLP
AVQRAAGLAP ALDTAAHAHA ATPPSRGPGS WEDHDMSGQS APRALAQTDA DTLHADGDAP
VHPLDDEQLA QSLDEAIARR VHFLTDYQDA AYAQQYRALV ERVRTHEAQR APGSTALSAA
VARYAFKLMA YKDEYEVARL YTRGDFQRRV QQQFEGDYQL RFHLAPPLFA KKDANGQPIK
REYGPWMFSA FKLLARLKFL RGGKLDVFGY TAERRGERQL IADYLATVNT LLQRLDNDNV
GLAAQIASIP EHIRGYGHVK DAHLHEAKAR EAALLAQWRN PKALHVVQAA
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