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Database: UniProt
Entry: H3RH83_PANSE
LinkDB: H3RH83_PANSE
Original site: H3RH83_PANSE 
ID   H3RH83_PANSE            Unreviewed;       387 AA.
AC   H3RH83;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   08-MAY-2019, entry version 32.
DE   SubName: Full=Chorismate mutase I/prephenate dehydratase {ECO:0000313|EMBL:EHT99241.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:EHT99241.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:EHT99241.1};
GN   Name=pheA {ECO:0000313|EMBL:EHT99241.1};
GN   ORFNames=CKS_1239 {ECO:0000313|EMBL:EHT99241.1};
OS   Pantoea stewartii subsp. stewartii DC283.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=660596 {ECO:0000313|EMBL:EHT99241.1, ECO:0000313|Proteomes:UP000005050};
RN   [1] {ECO:0000313|EMBL:EHT99241.1, ECO:0000313|Proteomes:UP000005050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC283 {ECO:0000313|EMBL:EHT99241.1,
RC   ECO:0000313|Proteomes:UP000005050};
RX   PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA   Wang X., Yang F., von Bodman S.B.;
RT   "The genetic and structural basis of two distinct terminal side branch
RT   residues in stewartan and amylovoran exopolysaccharides and their
RT   potential role in host adaptation.";
RL   Mol. Microbiol. 83:195-207(2012).
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHT99241.1}.
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DR   EMBL; AHIE01000027; EHT99241.1; -; Genomic_DNA.
DR   RefSeq; WP_006120702.1; NZ_CP017581.1.
DR   STRING; 66269.NL54_20885; -.
DR   EnsemblBacteria; EHT99241; EHT99241; CKS_1239.
DR   KEGG; pstw:DSJ_05465; -.
DR   PATRIC; fig|660596.6.peg.3400; -.
DR   KO; K14170; -.
DR   Proteomes; UP000005050; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
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   Complete proteome {ECO:0000313|Proteomes:UP000005050};
KW   Isomerase {ECO:0000313|EMBL:EHT99241.1};
KW   Lyase {ECO:0000313|EMBL:EHT99241.1}.
FT   BINDING      11     11       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      28     28       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      39     39       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      48     48       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      52     52       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      84     84       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      88     88       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        278    278       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   387 AA;  43433 MW;  69535BEE135767AC CRC64;
     MTPDNPLLAL REKISAVDEK LLTLLAERRL LAVEVAEAKL ATHRPVRDIE RERALIEHLI
     VLGKKHQLDA HYITRLFQLV IEDSVLTQQA LLQKNLNHPH AQAARIAFLG PKGSYSHLAA
     RQYAARHFDS MVECGCLKFH DIIKQVENNA ADYAVLPIEN TSSGSINDVY DLLQQTNLSI
     VGEMTLPIEH CMLVSGPSDL EQIETVYSHP QPFQQSSHFI NRFPHWNIVY TESTAAAMEK
     VAALNSPKVA AIGSEAGGEL YQLRVLERHL ANQQQNHTRF IVLARKPIDV SDQISAKTTL
     IMATSQQAGA LVDALLVLRQ HNLIMSKLES RPINGNPWEE MFYLDVQGNL QSEKMQQALE
     ELRAMTRSLK VLGCYPSENV IPVEPKQ
//
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