ID A0A1I7KB92_9HYPH Unreviewed; 149 AA. AC A0A1I7KB92; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 03-AUG-2022, entry version 11. 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=SAMN02799643_03382 {ECO:0000313|EMBL:SFU94697.1}; OS Methylobacterium sp. UNCCL125. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=1502759 {ECO:0000313|EMBL:SFU94697.1, ECO:0000313|Proteomes:UP000199260}; RN [1] {ECO:0000313|EMBL:SFU94697.1, ECO:0000313|Proteomes:UP000199260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UNCCL125 {ECO:0000313|EMBL:SFU94697.1, RC ECO:0000313|Proteomes:UP000199260}; RA de Groot N.N.; RL Submitted (OCT-2016) 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 --------------------------------------------------------------------------- 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; FPBW01000015; SFU94697.1; -; Genomic_DNA. DR RefSeq; WP_043382565.1; NZ_FPBW01000015.1. DR EnsemblBacteria; SFU94697; SFU94697; SAMN02799643_03382. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000199260; Unassembled WGS sequence. 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 {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}. FT REGION 102..103 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" 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 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; 16133 MW; 7CFCEE864C8BBA7E CRC64; MNDTILVLNG PNLNLLGKRQ PEIYGRETLA DVEALCRETA AGFGLTVDFR QSNAEHVLID AIHDFRVGSA GIVINAGAYT HTSVALLDAL NTCEVPVIEY HISNVHRREA FRHHSYISLA ATAVLAGFGT HGYALAIRHL AHLRAGKPA //