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Database: UniProt
Entry: Q8PA96_XANCP
LinkDB: Q8PA96_XANCP
Original site: Q8PA96_XANCP 
ID   Q8PA96_XANCP            Unreviewed;       406 AA.
AC   Q8PA96;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   31-JUL-2019, entry version 95.
DE   SubName: Full=p-protein {ECO:0000313|EMBL:AAM40885.1};
GN   Name=pheA {ECO:0000313|EMBL:AAM40885.1};
GN   OrderedLocusNames=XCC1590 {ECO:0000313|EMBL:AAM40885.1};
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 /
OS   NCPPB 528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM40885.1, ECO:0000313|Proteomes:UP000001010};
RN   [1] {ECO:0000313|EMBL:AAM40885.1, 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.,
RA   Almeida N.F.Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A.Jr., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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DR   EMBL; AE008922; AAM40885.1; -; Genomic_DNA.
DR   RefSeq; NP_636961.1; NC_003902.1.
DR   RefSeq; WP_011036772.1; NC_003902.1.
DR   STRING; 340.xcc-b100_2670; -.
DR   EnsemblBacteria; AAM40885; AAM40885; XCC1590.
DR   GeneID; 35546053; -.
DR   GeneID; 998224; -.
DR   KEGG; xcc:XCC1590; -.
DR   PATRIC; fig|190485.4.peg.1703; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   eggNOG; COG1605; LUCA.
DR   HOGENOM; HOG000018971; -.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   BioCyc; XCAM190485:XCC1590-MONOMER; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR010957; G/b/e-P-prot_chorismate_mutase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01807; CM_P2; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001010};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001010}.
FT   DOMAIN       45    137       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      137    313       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      325    402       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1     39       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     16     30       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   SITE        306    306       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   406 AA;  44098 MW;  F4C4C7C33875FE18 CRC64;
     MKESPPMAPK PKNTNAAGGT AKSATKASSK KATKLAGKDS AKPLATAAPV LADVRAKIDE
     IDRGIQALIA ERANFAHQVG KAKGKLAAAV DYYRPEREAQ VLRMVVDRNE GPLSDEVLVH
     VFREIMSACL AQQEPLKIGY LGPEGTFSQQ AVLKHFGRSA VGLPMATIEE VFQEVEAGNA
     DFGVVPVENS GQGTIQVTLD MFLTSNLKIC GEVELRVHQY LLSRNGRLED IERIYAHSQS
     FAQTAGWLRS HLPKVEKIAV SSNAEGARRA RNAEDAAAIG GESAAHVYGL KKVIMKSIED
     DDDNTTRFLV IGRQIFPSSG HDRTSVLVFI HDKPGALFDV LSPFARHGIS MNRIESRPSH
     QAKWEYGFFI DLAGHVEDES MKQALAELEA HSAQIKVLGS YPVAIP
//
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