ID AROQ_SHEDO Reviewed; 151 AA.
AC Q12J15;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 29-MAY-2013, entry version 56.
DE RecName: Full=3-dehydroquinate dehydratase;
DE Short=3-dehydroquinase;
DE EC=4.2.1.10;
DE AltName: Full=Type II DHQase;
GN Name=aroQ; OrderedLocusNames=Sden_3285;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate
CC intermediate (By similarity).
CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC biosynthesis; chorismate from D-erythrose 4-phosphate and
CC phosphoenolpyruvate: step 3/7.
CC -!- SUBUNIT: Homododecamer (By similarity).
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
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DR EMBL; CP000302; ABE56561.1; -; Genomic_DNA.
DR RefSeq; YP_564284.1; NC_007954.1.
DR ProteinModelPortal; Q12J15; -.
DR SMR; Q12J15; 6-149.
DR STRING; 318161.Sden_3285; -.
DR EnsemblBacteria; ABE56561; ABE56561; Sden_3285.
DR GeneID; 4019833; -.
DR KEGG; sdn:Sden_3285; -.
DR PATRIC; 23492658; VBISheDen79529_3453.
DR eggNOG; COG0757; -.
DR HOGENOM; HOG000217278; -.
DR KO; K03786; -.
DR OMA; RREPGHY; -.
DR ProtClustDB; PRK05395; -.
DR BioCyc; SDEN318161:GHKQ-3398-MONOMER; -.
DR UniPathway; UPA00053; UER00086.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:HAMAP.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:HAMAP.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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; DHquinase_II; 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;
KW Complete proteome; Lyase.
FT CHAIN 1 151 3-dehydroquinate dehydratase.
FT /FTId=PRO_1000097619.
FT REGION 102 103 Substrate binding (By similarity).
FT ACT_SITE 26 26 Proton acceptor (By similarity).
FT ACT_SITE 101 101 Proton donor (By similarity).
FT BINDING 75 75 Substrate (By similarity).
FT BINDING 81 81 Substrate (By similarity).
FT BINDING 88 88 Substrate (By similarity).
FT BINDING 112 112 Substrate (By similarity).
FT SITE 21 21 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 151 AA; 16384 MW; 4719A0DBF89A9243 CRC64;
MSTTVKILLL NGPNLNLLGR REPGHYGHQT LATIVSELST QAQQASVSLE HLQSNAEHEL
IDAIHATDAQ FIIINPAAFT HTSVALRDAL LGVAIPFIEV HLSNVHAREP FRQHSYFSDK
ALGVICGLGA QGYKFALQAA LSHLSDKQLQ S
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