(data stored in ACNUC7421 zone)

SWISSPROT: AROQ_PSEHT

ID   AROQ_PSEHT              Reviewed;         150 AA.
AC   Q3IDT2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 77.
DE   RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00169};
DE            Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00169};
DE            EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00169};
DE   AltName: Full=Type II DHQase {ECO:0000255|HAMAP-Rule:MF_00169};
GN   Name=aroQ {ECO:0000255|HAMAP-Rule:MF_00169};
GN   OrderedLocusNames=PSHAa0264;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate
CC       intermediate. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC       {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00169}.
DR   EMBL; CR954246; CAI85363.1; -; Genomic_DNA.
DR   RefSeq; WP_011326977.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDT2; -.
DR   SMR; Q3IDT2; -.
DR   STRING; 326442.PSHAa0264; -.
DR   EnsemblBacteria; CAI85363; CAI85363; PSHAa0264.
DR   GeneID; 32566684; -.
DR   KEGG; pha:PSHAa0264; -.
DR   eggNOG; ENOG4108Z38; Bacteria.
DR   eggNOG; COG0757; LUCA.
DR   HOGENOM; HOG000217278; -.
DR   KO; K03786; -.
DR   OMA; AYTHYSY; -.
DR   OrthoDB; POG091H03XJ; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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; Q3IDT2.
DR   SWISS-2DPAGE; Q3IDT2.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Reference proteome.
FT   CHAIN         1    150       3-dehydroquinate dehydratase.
FT                                /FTId=PRO_1000023497.
FT   REGION      104    105       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00169}.
FT   ACT_SITE     26     26       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00169}.
FT   ACT_SITE    103    103       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00169}.
FT   BINDING      77     77       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00169}.
FT   BINDING      83     83       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00169}.
FT   BINDING      90     90       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00169}.
FT   BINDING     114    114       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00169}.
FT   SITE         21     21       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00169}.
SQ   SEQUENCE   150 AA;  16596 MW;  80D20361DBF12F70 CRC64;
     MAAKFKLLVI NGPNLNMLGK REPDKYGSRT LSEIMSELTC AADSLNVELT HFQSNSEQAL
     IERIHDTWQA IDYIIINPAA FTHTSVALRD ALLSVDIPFF EVHLSNVHAR EAFRHHSYFS
     DVAQGVICGL GAMGYHAALE AAVNQLQNSN
//

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