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Database: UniProt
Entry: B6EGD1_ALISL
LinkDB: B6EGD1_ALISL
Original site: B6EGD1_ALISL 
ID   B6EGD1_ALISL            Unreviewed;       391 AA.
AC   B6EGD1;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   16-JAN-2019, entry version 57.
DE   SubName: Full=p-protein {ECO:0000313|EMBL:CAQ78346.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:CAQ78346.1};
GN   Name=pheA {ECO:0000313|EMBL:CAQ78346.1};
GN   OrderedLocusNames=VSAL_I0661 {ECO:0000313|EMBL:CAQ78346.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ78346.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ78346.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ78346.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S.,
RA   Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A.,
RA   Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida
RT   strain LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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DR   EMBL; FM178379; CAQ78346.1; -; Genomic_DNA.
DR   RefSeq; WP_012549467.1; NC_011312.1.
DR   STRING; 316275.VSAL_I0661; -.
DR   EnsemblBacteria; CAQ78346; CAQ78346; VSAL_I0661.
DR   KEGG; vsa:VSAL_I0661; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   eggNOG; COG1605; LUCA.
DR   HOGENOM; HOG000018972; -.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   OrthoDB; 1280729at2; -.
DR   Proteomes; UP000001730; 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:UniProtKB-EC.
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:UP000001730};
KW   Lyase {ECO:0000313|EMBL:CAQ78346.1}.
FT   DOMAIN        2     93       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      108    288       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      302    379       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      85     85       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      89     89       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        281    281       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   391 AA;  44059 MW;  857B2021091A162B CRC64;
     MTDTHYSLDD IRLRLNDLDN ELLKLFSERR KLSLKVAKSK VQTSKPVRDS KREQQLLVKL
     IKNGKAFDLD AHYITQIFHT IIEDSVLLQQ EYFQNLANPE LSRKPIARVA YLGSKGSYSN
     LASRRYFSKK NTELAELGCE NFREVIKTVE SGHADYGVLP IENTSSGSIN EVYDLLQHTS
     LYIVGELTQK IDHCLLTTSE TSLEQITTLY SHPQPHQQCS EFLNRLDNVE LISCSSTADA
     MIMVKDINSP TVAAIGNSDS GKLYSLQQLI TNISNQTENQ TRFIVVARKP VDVSEQIPAK
     TTLIMSTSQD AGSLVESLLV LRKYGINMTK LESRPIMGNP WEEMFYIDLE AHLKSDAMNS
     AIEELTSITQ YLKVLGCYPI ENVTPTTIPL T
//
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