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Database: UniProt
Entry: E2PVJ9_STRC2
LinkDB: E2PVJ9_STRC2
Original site: E2PVJ9_STRC2 
ID   E2PVJ9_STRC2            Unreviewed;       311 AA.
AC   E2PVJ9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   11-DEC-2019, entry version 30.
DE   SubName: Full=Putative prephenate dehydratase {ECO:0000313|EMBL:EFG07913.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:EFG07913.1};
GN   ORFNames=SCLAV_2840 {ECO:0000313|EMBL:EFG07913.1};
OS   Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / NBRC
OS   13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=443255 {ECO:0000313|EMBL:EFG07913.1, ECO:0000313|Proteomes:UP000002357};
RN   [1] {ECO:0000313|EMBL:EFG07913.1, ECO:0000313|Proteomes:UP000002357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC   NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX   PubMed=20624727; DOI=10.1093/gbe/evq013;
RA   Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA   Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA   Breitling R., Takano E.;
RT   "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT   evolutionary reservoir of secondary metabolic pathways.";
RL   Genome Biol. Evol. 2:212-224(2010).
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DR   EMBL; CM000913; EFG07913.1; -; Genomic_DNA.
DR   RefSeq; WP_003961075.1; NZ_CP027858.1.
DR   STRING; 443255.SCLAV_2840; -.
DR   EnsemblBacteria; EFG07913; EFG07913; SCLAV_2840.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   OMA; REVMSAC; -.
DR   OrthoDB; 1280729at2; -.
DR   Proteomes; UP000002357; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:EFG07913.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT   DOMAIN          5..183
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          198..273
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            176
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   311 AA;  33097 MW;  D2CBE2299672C1BD CRC64;
     MSATRYTYLG PEGTFTEAAL RTLPEAATRE LVPMVSVPAA LDAVRNGDAA AALVPIENSV
     EGGVTATLDE LASGTPLMIY REVLLPIAFA LLVRPGTRLS DVRTVTGHPV AQPQVRNWLR
     ANLPDALWES AASNADGARL VKEGKYDAAF AGEFAAATYG LEALVTDIHD AQNAETRFVL
     VGRPARPAAP TGADRTSVVI WLGTDRPGAL LELLQEFAVR GVNLMLIQSR PTGEGIGNYC
     FAVDAEGHIT ERRVAEALMG LKRTAPKVRF LGSYPRAGVT PDKVSKPRAG TSDADFTEAS
     DWLGRCQDGR G
//
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