ID AROD_SHISS Reviewed; 252 AA.
AC Q3Z247;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 29-MAY-2013, entry version 54.
DE RecName: Full=3-dehydroquinate dehydratase;
DE Short=3-dehydroquinase;
DE EC=4.2.1.10;
DE AltName: Full=Type I DHQase;
GN Name=aroD; OrderedLocusNames=SSON_1461;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
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DR EMBL; CP000038; AAZ88165.1; -; Genomic_DNA.
DR RefSeq; YP_310400.1; NC_007384.1.
DR ProteinModelPortal; Q3Z247; -.
DR SMR; Q3Z247; 1-252.
DR STRING; 300269.SSON_1461; -.
DR EnsemblBacteria; AAZ88165; AAZ88165; SSON_1461.
DR GeneID; 3670791; -.
DR KEGG; ssn:SSON_1461; -.
DR PATRIC; 18736796; VBIShiSon107113_1748.
DR eggNOG; COG0710; -.
DR HOGENOM; HOG000105514; -.
DR KO; K03785; -.
DR OMA; IIEWRVD; -.
DR ProtClustDB; PRK02412; -.
DR BioCyc; SSON300269:GJJF-1457-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; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1; -.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001381; DHquinase_I.
DR Pfam; PF01487; DHquinase_I; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
DR PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Lyase; Schiff base.
FT CHAIN 1 252 3-dehydroquinate dehydratase.
FT /FTId=PRO_1000043184.
FT REGION 46 48 Substrate binding (By similarity).
FT ACT_SITE 143 143 Proton donor/acceptor (By similarity).
FT ACT_SITE 170 170 Schiff-base intermediate with substrate
FT (By similarity).
FT BINDING 82 82 Substrate (By similarity).
FT BINDING 213 213 Substrate (By similarity).
FT BINDING 232 232 Substrate (By similarity).
FT BINDING 236 236 Substrate (By similarity).
SQ SEQUENCE 252 AA; 27520 MW; 1B02F00074A56C3F CRC64;
MKTVTVKDLV IGAGAPKIIV SLMAKDIARV KSEALAYREA DFDILEWRVD HFADLSNVES
VMAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL NRAAIDSGLV DMIDLELFTG
DDQVKETVAY AHAHDVKVVM SNHDFHKTPE AEEIIARLRK MQSFDADIPK IALMPQSTSD
VLTLLTATLE MQEQYADRPI ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVN
DLRTVLTILH QA
//
