ID A0A417H8J1_9CLOT Unreviewed; 144 AA. AC A0A417H8J1; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078243}; 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:SAAS01078243}; 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. 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 RT microbiota."; RL Submitted (AUG-2018) 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: 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00169, ECO:0000256|SAAS:SAAS01115812}; 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 ECO:0000256|SAAS:SAAS01078239}. CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078241}. 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: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 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 Complete proteome {ECO:0000313|Proteomes:UP000283242}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078240, KW ECO:0000313|EMBL:RHT68092.1}. FT REGION 101 102 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00169}. FT ACT_SITE 23 23 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT ACT_SITE 100 100 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT BINDING 74 74 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT BINDING 80 80 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT BINDING 87 87 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT BINDING 111 111 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00169}. FT SITE 18 18 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00169}. SQ SEQUENCE 144 AA; 15546 MW; CE8E148651B11025 CRC64; MKKVLLIHGP NLNLTGQREP GIYGSNTLAS INAEVVQKCE RLGMECAVFQ SNSEGALIDR IHAAREDCDA IIMNAGAYTH YSYAIRDAIA AVRLPCVEVH MSNVHAREEF RHKSVIGPVC AGVIAGFGKH SYLLAVDAVK SIIG //