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Database: UniProt
Entry: G7UVX4_PSEUP
LinkDB: G7UVX4_PSEUP
Original site: G7UVX4_PSEUP 
ID   G7UVX4_PSEUP            Unreviewed;       386 AA.
AC   G7UVX4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   16-JAN-2019, entry version 34.
DE   SubName: Full=Putative bifunctional chorismate mutase/prephenate dehydratase {ECO:0000313|EMBL:AER56443.1};
GN   OrderedLocusNames=DSC_08965 {ECO:0000313|EMBL:AER56443.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER56443.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER56443.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER56443.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium
RT   Pseudoxanthomonas spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
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DR   EMBL; CP003093; AER56443.1; -; Genomic_DNA.
DR   RefSeq; WP_014160619.1; NC_016147.2.
DR   STRING; 1045855.DSC_08965; -.
DR   EnsemblBacteria; AER56443; AER56443; DSC_08965.
DR   KEGG; psd:DSC_08965; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   eggNOG; COG1605; LUCA.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; PSPA1045855:G1H1D-1589-MONOMER; -.
DR   Proteomes; UP000005870; 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; IEA:InterPro.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
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   InterPro; IPR018528; Preph_deHydtase_CS.
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; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005870};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT   DOMAIN       25    117       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      117    293       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      305    382       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED       31     51       {ECO:0000256|SAM:Coils}.
FT   SITE        286    286       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   386 AA;  42141 MW;  04F2328A5A4A391B CRC64;
     MTNKSTKPAA AKAKPVAKPA KAPAVVAAPA LSDVRAKIDS IDRQIQALIA ERARFAHQVG
     KAKGKLAAAV DYYRPEREAQ VLRMVIDRNE GPLSDELLVH VFREIMSACL AQQEPLKIGY
     LGPEGTFSQQ AVLKHFGRSA LGLPMASIEE VFQEVENGNA DFGVVPVENS GQGTIQITLD
     MFLTSNLKIC GEVELRVQQY LMSRSGRLED IERVYAHPQS FMQTSGWLRA NLPKAEKVPV
     SSNAEGARRA RNSDDAAAIG GESAVHAYGL KKVVMSPIQD DKDNTTRFLV VGRQIFPSSG
     HDRTSVLVFI HDKPGALFDV LSPFARHGIS MSRIESRPSL HAKWEYGFFI DLAGHVEDEP
     MKLALAELKA HSAQIKVLGS YPVAVP
//
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