ID A0A417H8J1_9CLOT Unreviewed; 144 AA. AC A0A417H8J1; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 07-APR-2021, entry version 7. 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 ECO:0000313|EMBL:RHT68092.1}; GN ORFNames=DW742_15260 {ECO:0000313|EMBL:RHT68092.1}; OS Butyricicoccus sp. AM28-25. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Butyricicoccus; unclassified Butyricicoccus. OX NCBI_TaxID=2292294 {ECO:0000313|EMBL:RHT68092.1, ECO:0000313|Proteomes:UP000283242}; RN [1] {ECO:0000313|EMBL:RHT68092.1, ECO:0000313|Proteomes:UP000283242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM28-25 {ECO:0000313|EMBL:RHT68092.1, RC ECO:0000313|Proteomes:UP000283242}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. CC {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:RHT68092.1}. 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; QUJL01000024; RHT68092.1; -; Genomic_DNA. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000283242; 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 101..102 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT ACT_SITE 23 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-1" FT ACT_SITE 100 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-1" FT BINDING 74 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT BINDING 80 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT BINDING 87 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT BINDING 111 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-2" FT SITE 18 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00169, FT ECO:0000256|PIRSR:PIRSR001399-3" SQ SEQUENCE 144 AA; 15546 MW; CE8E148651B11025 CRC64; MKKVLLIHGP NLNLTGQREP GIYGSNTLAS INAEVVQKCE RLGMECAVFQ SNSEGALIDR IHAAREDCDA IIMNAGAYTH YSYAIRDAIA AVRLPCVEVH MSNVHAREEF RHKSVIGPVC AGVIAGFGKH SYLLAVDAVK SIIG //