(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKI2_PSEAB

ID   A0A0H2ZKI2_PSEAB        Unreviewed;       148 AA.
AC   A0A0H2ZKI2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 15.
DE   RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS00734288};
DE            Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00169};
DE            EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS00734288};
DE   AltName: Full=Type II DHQase {ECO:0000256|HAMAP-Rule:MF_00169};
GN   Name=aroQ2 {ECO:0000313|EMBL:ABJ15194.1};
GN   Synonyms=aroQ {ECO:0000256|HAMAP-Rule:MF_00169};
GN   OrderedLocusNames=PA14_03030 {ECO:0000313|EMBL:ABJ15194.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15194.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15194.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15194.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate
CC       intermediate. {ECO:0000256|HAMAP-Rule:MF_00169}.
CC   -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC       {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS00734301}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_00169}.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000256|HAMAP-Rule:MF_00169,
CC       ECO:0000256|SAAS:SAAS00734325}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS00734308}.
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DR   EMBL; CP000438; ABJ15194.1; -; Genomic_DNA.
DR   RefSeq; WP_003137122.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15194; ABJ15194; PA14_03030.
DR   KEGG; pau:PA14_03030; -.
DR   KO; K03786; -.
DR   OMA; CAGIVIN; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00466; DHQase_II; 1.
DR   Gene3D; 3.40.50.9100; -; 1.
DR   HAMAP; MF_00169; AroQ; 1.
DR   InterPro; IPR001874; DHquinase_II.
DR   InterPro; IPR018509; DHquinase_II_CS.
DR   PANTHER; PTHR21272; PTHR21272; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; DHquinase_II; 1.
DR   ProDom; PD004527; DHquinase_II; 1.
DR   SUPFAM; SSF52304; SSF52304; 1.
DR   TIGRFAMs; TIGR01088; aroQ; 1.
DR   PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZKI2.
DR   SWISS-2DPAGE; A0A0H2ZKI2.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00169};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00169};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00169,
KW   ECO:0000256|SAAS:SAAS00734332}.
FT   REGION      102    103       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00169, ECO:0000256|PIRSR:
FT                                PIRSR001399-2}.
FT   ACT_SITE     24     24       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                1}.
FT   ACT_SITE    101    101       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                1}.
FT   BINDING      75     75       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING      81     81       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING      88     88       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING     112    112       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   SITE         19     19       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00169,
FT                                ECO:0000256|PIRSR:PIRSR001399-3}.
SQ   SEQUENCE   148 AA;  16286 MW;  051D32D0ECE655E3 CRC64;
     MTRTVLVLNG PNLNLLGIRE PQTYGRRTLG EIADECAAFA ETRGFAVDFR QTNQEGQLLD
     WIHQARGRVA GIVINPAAWT HTSVALRDAL AAVELPVVEV HLSNVHQREA FRHHSYVSPV
     ALGVICGFGS LGYRLALEHF AERFEAAA
//

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