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Database: UniProt
Entry: E1QE66_DESB2
LinkDB: E1QE66_DESB2
Original site: E1QE66_DESB2 
ID   E1QE66_DESB2            Unreviewed;       410 AA.
AC   E1QE66;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   13-NOV-2019, entry version 45.
DE   SubName: Full=Prephenate dehydratase {ECO:0000313|EMBL:ADK83852.1};
GN   OrderedLocusNames=Deba_0479 {ECO:0000313|EMBL:ADK83852.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / VKM B-1802 /
OS   2st14).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83852.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK83852.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Han C., Rohde M., Brambilla E., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain
RT   (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
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DR   EMBL; CP002085; ADK83852.1; -; Genomic_DNA.
DR   STRING; 644282.Deba_0479; -.
DR   EnsemblBacteria; ADK83852; ADK83852; Deba_0479.
DR   KEGG; dbr:Deba_0479; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   HOGENOM; HOG000018971; -.
DR   KO; K14170; -.
DR   OMA; QGVGAIC; -.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; DBAA644282:G1GM5-481-MONOMER; -.
DR   Proteomes; UP000009047; 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; 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:UP000009047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT   DOMAIN       42    132       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      132    307       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      319    396       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED       48     68       {ECO:0000256|SAM:Coils}.
FT   SITE        300    300       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   410 AA;  45195 MW;  259C68F7063BA4F9 CRC64;
     MTDRTPFFAG LTLGLAGGRN RRPNQKAAHL RPVYPPRQEN HDMVADQINQ QRQRIDEIDR
     QIVDLLNERA LCAMAIGRSK NAGGLPEFAP EREQAIIDAL ERHNQGPLSG QSLRGIFAEI
     ISACRAVQRP LRVAFLGPAT TFSHQAAMRH FGSSCEFAPH RSIIDVFHEV ERSHAQVGVV
     PVENSSEGQV SVTLDLFLES DLNVCGEIYA RISQVLMSKE AAIEGIQRVY SHPQALNQCR
     NWLARNMPMA TLIESTSTAA AAQKAAQEDG SAAVGSILAA RQGGLNALAI DIQDNPHNTT
     RFFVIGRQKC PPTGNDKTSI LFVTHHKPGM LFSALKHFAD SGINLTRIES RPLKNTPWEY
     VFFIDMAGHV EDAQVRQVIN TLDEETRLLK VLGSYPMGEP EAWNGAEQAV
//
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