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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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