ID A0A0F3IQG5_9PROT Unreviewed; 149 AA. AC A0A0F3IQG5; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 02-OCT-2024, entry version 34. DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|ARBA:ARBA00012060, ECO:0000256|HAMAP-Rule:MF_00169}; DE Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00169}; DE EC=4.2.1.10 {ECO:0000256|ARBA:ARBA00012060, ECO:0000256|HAMAP-Rule:MF_00169}; 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; Pseudomonadota; 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, ECO:0000313|Proteomes:UP000033774} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Dia-1 {ECO:0000313|EMBL:KJV08990.1, RC ECO:0000313|Proteomes:UP000033774}; 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 intermediate. CC {ECO:0000256|ARBA:ARBA00003924, 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; CC Evidence={ECO:0000256|ARBA:ARBA00001864, ECO:0000256|HAMAP- CC Rule:MF_00169}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 3/7. {ECO:0000256|ARBA:ARBA00004902, ECO:0000256|HAMAP-Rule:MF_00169}. CC -!- SUBUNIT: Homododecamer. {ECO:0000256|ARBA:ARBA00011193, CC ECO:0000256|HAMAP-Rule:MF_00169}. CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC {ECO:0000256|ARBA:ARBA00011037, ECO:0000256|HAMAP-Rule:MF_00169}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A0F3IQG5; -. DR PATRIC; fig|552518.3.peg.2597; -. DR OrthoDB; 9790793at2; -. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000033774; Unassembled WGS sequence. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00466; DHQase_II; 1. DR Gene3D; 3.40.50.9100; Dehydroquinase, class II; 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 NCBIfam; TIGR01088; aroQ; 1. DR PANTHER; PTHR21272; CATABOLIC 3-DEHYDROQUINASE; 1. DR PANTHER; PTHR21272:SF3; CATABOLIC 3-DEHYDROQUINASE; 1. DR Pfam; PF01220; DHquinase_II; 1. DR PIRSF; PIRSF001399; DHquinase_II; 1. DR SUPFAM; SSF52304; Type II 3-dehydroquinate dehydratase; 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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00169}; KW Reference proteome {ECO:0000313|Proteomes:UP000033774}. FT ACT_SITE 24 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-1" FT ACT_SITE 101 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-1" FT BINDING 75 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT BINDING 81 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT BINDING 88 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT BINDING 102..103 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT BINDING 112 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT SITE 19 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-3" SQ SEQUENCE 149 AA; 15898 MW; 8F7AC98B758163FC CRC64; MTPCVFVLNG PNLNLLGTRQ PHIYGSATLA DVAAACAVTA DTLGLGVRFH QSNHEAALID WVHEARTAAQ AIVINPAAYT HTSVALLDAL NAFEGPVIEV HISNIHKRES FRHQSYVSLR ADGIIAGLGT QGYTLALQRV AHLLAEAAR //