ID M0BBD6_9EURY Unreviewed; 233 AA. AC M0BBD6; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 14-DEC-2022, entry version 38. DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_00214}; DE Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00214}; DE EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_00214}; DE AltName: Full=Type I DHQase {ECO:0000256|HAMAP-Rule:MF_00214}; DE AltName: Full=Type I dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00214}; DE Short=DHQ1 {ECO:0000256|HAMAP-Rule:MF_00214}; GN Name=aroD {ECO:0000256|HAMAP-Rule:MF_00214}; GN ORFNames=C479_12858 {ECO:0000313|EMBL:ELZ08231.1}; OS Halovivax asiaticus JCM 14624. OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales; OC Natrialbaceae; Halovivax. OX NCBI_TaxID=1227490 {ECO:0000313|EMBL:ELZ08231.1, ECO:0000313|Proteomes:UP000011560}; RN [1] {ECO:0000313|EMBL:ELZ08231.1, ECO:0000313|Proteomes:UP000011560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 14624 {ECO:0000313|EMBL:ELZ08231.1, RC ECO:0000313|Proteomes:UP000011560}; RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D., RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals RT strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). CC -!- FUNCTION: Involved in the third step of the chorismate pathway, which CC leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- CC dehydration of 3-dehydroquinate (DHQ) and introduces the first double CC bond of the aromatic ring to yield 3-dehydroshikimate. CC {ECO:0000256|HAMAP-Rule:MF_00214}. 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_00214}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 3/7. {ECO:0000256|HAMAP-Rule:MF_00214}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00214}. CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family. CC {ECO:0000256|HAMAP-Rule:MF_00214}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00214}. 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:ELZ08231.1}. 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; AOIQ01000021; ELZ08231.1; -; Genomic_DNA. DR RefSeq; WP_007703299.1; NZ_AOIQ01000021.1. DR AlphaFoldDB; M0BBD6; -. DR STRING; 1227490.C479_12858; -. DR EnsemblBacteria; ELZ08231; ELZ08231; C479_12858. DR PATRIC; fig|1227490.4.peg.2615; -. DR OrthoDB; 75928at2157; -. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000011560; 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-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00502; DHQase_I; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00214; AroD; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001381; DHquinase_I. DR Pfam; PF01487; DHquinase_I; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00214}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00214}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00214}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00214}. FT ACT_SITE 118 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214" FT ACT_SITE 144 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214" FT BINDING 29..31 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214" FT BINDING 56 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214" FT BINDING 185 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214" FT BINDING 206 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214" FT BINDING 210 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214" SQ SEQUENCE 233 AA; 24086 MW; A1929F3AD77F2648 CRC64; MNFESFVLAA STATLADEPR ARAHADAIEF RLDLADEPLA QLARYDGELP ILATNRPTWE GGARSGDERS RLDTLAEATT VDAVAAIDVE LAAIRAGTAG RLLDAAREND VAVVVSVHDF DGTSSLSTLL ALLEAAGAHG AVAKLAVTAE SPADTLTLLR ATHEATAAGQ PVATMAMGEL GSHTRAVAPV YGSRIGYAPL DPAATTAPGQ LDLATLATTI ESVVAPHRSK REN //