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Database: UniProt
Entry: M1P6S9_DESSD
LinkDB: M1P6S9_DESSD
Original site: M1P6S9_DESSD 
ID   M1P6S9_DESSD            Unreviewed;       362 AA.
AC   M1P6S9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   05-JUN-2019, entry version 30.
DE   SubName: Full=Prephenate dehydratase {ECO:0000313|EMBL:AGF79168.1};
GN   OrderedLocusNames=UWK_02632 {ECO:0000313|EMBL:AGF79168.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF79168.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M.,
RA   Amann R., Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic
RT   sulfur compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
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DR   EMBL; CP003985; AGF79168.1; -; Genomic_DNA.
DR   RefSeq; WP_015404854.1; NC_020304.1.
DR   STRING; 1167006.UWK_02632; -.
DR   EnsemblBacteria; AGF79168; AGF79168; UWK_02632.
DR   KEGG; dsf:UWK_02632; -.
DR   PATRIC; fig|1167006.5.peg.2850; -.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; DSUL1167006:G1HFC-2622-MONOMER; -.
DR   Proteomes; UP000011721; Chromosome.
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; 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   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000011721};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT   DOMAIN        1     89       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN       89    264       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      276    353       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   BINDING       9      9       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      26     26       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      37     37       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      46     46       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      50     50       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      81     81       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      85     85       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        257    257       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   362 AA;  40253 MW;  8067D4A8BBBF7166 CRC64;
     MAKDLTPVRD GIDKIDNTIL ELLKERLSLA KSIGQLKDES KRAKWDPLRE RQIYERLTKL
     NDGVFPDNSL HSIFHEIITT CRLSQQKIAV AYLGPEATFT HLAGVKYFGQ SATYSPMESI
     ADVFSEVEKG RTQYGIVPVE NSIEGAVFST LDSFMQYRTK ICGEVRMEIT HNLVCKSGDI
     SDIQTVASHT QPLAQCREWL RKHLPSCPTL PVFSTGAAAQ MAANNPNIGA IASSLAIKTY
     DLQVVVRGIE DYRGNTTRFL VIGKESPSPS GADRTSLLLG IMERPGALNE ILSVIARAGI
     NLAKIESRPI KGKQWKYLFF LDLMGHIEDE HIKDCCKTLN SLCSYYEWLG SYPQADESSS
     DA
//
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