(data stored in SCRATCH zone)

SWISSPROT: B2TD27_PARPJ

ID   B2TD27_PARPJ            Unreviewed;       151 AA.
AC   B2TD27;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078243};
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:SAAS01078243};
DE   AltName: Full=Type II DHQase {ECO:0000256|HAMAP-Rule:MF_00169};
GN   Name=aroQ {ECO:0000256|HAMAP-Rule:MF_00169};
GN   OrderedLocusNames=Bphyt_4568 {ECO:0000313|EMBL:ACD18941.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18941.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD18941.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate
CC       intermediate. {ECO:0000256|HAMAP-Rule:MF_00169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00169, ECO:0000256|SAAS:SAAS01115812};
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:SAAS01078239}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078241}.
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DR   EMBL; CP001053; ACD18941.1; -; Genomic_DNA.
DR   RefSeq; WP_012426455.1; NC_010676.1.
DR   STRING; 398527.Bphyt_4568; -.
DR   EnsemblBacteria; ACD18941; ACD18941; Bphyt_4568.
DR   KEGG; bpy:Bphyt_4568; -.
DR   eggNOG; ENOG4108Z38; Bacteria.
DR   eggNOG; COG0757; LUCA.
DR   HOGENOM; HOG000217278; -.
DR   KO; K03786; -.
DR   OMA; CAGIVIN; -.
DR   OrthoDB; 1872106at2; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001739; Chromosome 2.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
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   InterPro; IPR036441; DHquinase_II_sf.
DR   PANTHER; PTHR21272; PTHR21272; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; 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; B2TD27.
DR   SWISS-2DPAGE; B2TD27.
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:UP000001739};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078240,
KW   ECO:0000313|EMBL:ACD18941.1}.
FT   REGION      103    104       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00169, ECO:0000256|PIRSR:
FT                                PIRSR001399-2}.
FT   ACT_SITE     25     25       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                1}.
FT   ACT_SITE    102    102       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                1}.
FT   BINDING      76     76       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING      82     82       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING      89     89       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING     113    113       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   SITE         20     20       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00169,
FT                                ECO:0000256|PIRSR:PIRSR001399-3}.
SQ   SEQUENCE   151 AA;  16416 MW;  E7C932A61DE3233E CRC64;
     MSFASVLVLN GPNLNLLGTR EPAIYGSETL DDVAKLCRDA AERLDLSINF CQSNAEHQLI
     DWLHAARTKV DGIVINPAAY THTSVAIADA LTAIEKPVVE VHISNVHRRE AFRHHSYVSA
     VADAIIIGCG TQGYVLALER MATILKNRAA K
//

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