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Database: UniProt
Entry: Q87S69_VIBPA
LinkDB: Q87S69_VIBPA
Original site: Q87S69_VIBPA 
ID   Q87S69_VIBPA            Unreviewed;       392 AA.
AC   Q87S69;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   SubName: Full=Chorismate mutase/prephenate dehydratase {ECO:0000313|EMBL:BAC58818.1};
GN   OrderedLocusNames=VP0555 {ECO:0000313|EMBL:BAC58818.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC58818.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC58818.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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DR   EMBL; BA000031; BAC58818.1; -; Genomic_DNA.
DR   RefSeq; NP_796934.1; NC_004603.1.
DR   RefSeq; WP_005468591.1; NC_004603.1.
DR   STRING; 223926.28805538; -.
DR   PRIDE; Q87S69; -.
DR   EnsemblBacteria; BAC58818; BAC58818; BAC58818.
DR   GeneID; 1188023; -.
DR   KEGG; vpa:VP0555; -.
DR   PATRIC; fig|223926.6.peg.527; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   eggNOG; COG1605; LUCA.
DR   HOGENOM; HOG000018972; -.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   BioCyc; VPAR223926:G1GTB-567-MONOMER; -.
DR   Proteomes; UP000002493; Chromosome 1.
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; IPR010952; CM_P_1.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
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; TIGR01797; CM_P_1; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 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:UP000002493};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002493}.
FT   DOMAIN        2     94       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      109    289       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      303    380       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED        8     35       {ECO:0000256|SAM:Coils}.
FT   BINDING      12     12       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      29     29       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      40     40       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      49     49       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      53     53       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      86     86       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      90     90       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        282    282       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   392 AA;  44224 MW;  067FEFFCD15E0194 CRC64;
     MTDQPISLEE IRLRLNELDD QLLSLLSERR KLSIEVAKSK VQTSKPVRDA VREQQLLVKL
     ISNGRDKYEL DAQYITKLFH TIIEDSVLLQ QGYLQNLVNP QQSRKPLARV AFLGAKGSYS
     HLASREYFSR KNTELIELNC EHFKEVTRTV ESGHADYGVL PIENTSSGSI NEVYDLLQHT
     TLYIVGELTQ PIEHCLVATK DIRLEDIKTL YSHPQPHQQC SEFLSRMKGV KLESCASTAD
     AMQKVQEMNR DDVAAIGNAS SGKLYGLQAI QGNIANQTEN HTRFIVVARK PVEVSTQIPA
     KTTLIMSTSQ EAGSLVETLL VLQRYGINMT KLESRPIMGN PWEEMFYVDL EAHLGSTEMQ
     QALQELTKIT KHLKVLGCYP SENIKPTQVK LS
//
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