AROQ2_PSEPK
ID AROQ2_PSEPK Reviewed; 149 AA.
AC Q88K84;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=3-dehydroquinate dehydratase 2;
DE Short=3-dehydroquinase 2;
DE EC=4.2.1.10;
DE AltName: Full=Type II DHQase 2;
GN Name=aroQ2; Synonyms=aroQ-2; OrderedLocusNames=PP_2407;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7.
CC -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000305}.
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DR EMBL; AE015451; AAN68019.1; -; Genomic_DNA.
DR RefSeq; NP_744555.1; NC_002947.4.
DR RefSeq; WP_003250469.1; NC_002947.4.
DR AlphaFoldDB; Q88K84; -.
DR SMR; Q88K84; -.
DR STRING; 160488.PP_2407; -.
DR EnsemblBacteria; AAN68019; AAN68019; PP_2407.
DR KEGG; ppu:PP_2407; -.
DR PATRIC; fig|160488.4.peg.2550; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_2_0_6; -.
DR OMA; CAGIVIN; -.
DR PhylomeDB; Q88K84; -.
DR BioCyc; PPUT160488:G1G01-2570-MON; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000000556; Chromosome.
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:0008652; P:cellular amino acid 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 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;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome.
FT CHAIN 1..149
FT /note="3-dehydroquinate dehydratase 2"
FT /id="PRO_0000159921"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 149 AA; 16211 MW; D10A4D670DA9D124 CRC64;
MKPLILVLNG PNLNMLGTRE PAQYGHETLA DLAQGCADTA HAHGLEIEFR QTNHEGELID
WIHAARGRCA GIVINPGAWT HTSVAIRDAL VASELPVIEV HLSNVHKREP FRHLSFVSSI
AVGVICGLGS HGYRMALSHF AELLQERAA
