ID A0A0F3IQG5_9PROT Unreviewed; 149 AA. AC A0A0F3IQG5; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 22-JUL-2015, entry version 2. DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS00027752}; 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:SAAS00027752}; DE AltName: Full=Type II DHQase {ECO:0000256|HAMAP-Rule:MF_00169}; GN Name=aroQ {ECO:0000256|HAMAP-Rule:MF_00169}; GN ORFNames=VZ95_14235 {ECO:0000313|EMBL:KJV08990.1}; OS Elstera litoralis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Elstera. OX NCBI_TaxID=552518 {ECO:0000313|EMBL:KJV08990.1, ECO:0000313|Proteomes:UP000033774}; RN [1] {ECO:0000313|EMBL:KJV08990.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dia-1 {ECO:0000313|EMBL:KJV08990.1}; RA Rahalkar M.C., Dhakephalkar P.K., Pore S.D., Arora P., Kapse N.G., RA Pandit P.S.; RT "Draft genome sequence of Elstera litoralis."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate CC intermediate. {ECO:0000256|HAMAP-Rule:MF_00169}. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS00027731}. 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 -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC {ECO:0000256|HAMAP-Rule:MF_00169}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJV08990.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LAJY01000391; KJV08990.1; -; Genomic_DNA. DR RefSeq; WP_045776447.1; NZ_LAJY01000391.1. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000033774; Unassembled WGS sequence. 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; SSF52304; 1. DR TIGRFAMs; TIGR01088; aroQ; 1. DR PROSITE; PS01029; DEHYDROQUINASE_II; 1. PE 3: Inferred from homology; 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:UP000033774}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00169, KW ECO:0000256|SAAS:SAAS00027746}. FT REGION 102 103 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00169}. FT ACT_SITE 24 24 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT ACT_SITE 101 101 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT BINDING 75 75 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT BINDING 81 81 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT BINDING 88 88 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT BINDING 112 112 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT SITE 19 19 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00169}. SQ SEQUENCE 149 AA; 15898 MW; 8F7AC98B758163FC CRC64; MTPCVFVLNG PNLNLLGTRQ PHIYGSATLA DVAAACAVTA DTLGLGVRFH QSNHEAALID WVHEARTAAQ AIVINPAAYT HTSVALLDAL NAFEGPVIEV HISNIHKRES FRHQSYVSLR ADGIIAGLGT QGYTLALQRV AHLLAEAAR //