ID AROD_SALTY Reviewed; 252 AA. AC P58687; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214}; DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214}; DE Short=DHQD {ECO:0000303|PubMed:21291284}; DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:21291284, ECO:0000269|PubMed:23341204, ECO:0000269|PubMed:24957267}; DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214}; DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214}; DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214}; GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214}; GN OrderedLocusNames=STM1358; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [2] RP ACTIVE SITE. RX PubMed=22847490; DOI=10.1039/c2ob25605c; RA Yao Y., Li Z.S.; RT "New insights into the mechanism of the Schiff base hydrolysis catalyzed by RT type I dehydroquinate dehydratase from S. enterica: a theoretical study."; RL Org. Biomol. Chem. 10:7037-7044(2012). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=24957267; DOI=10.1042/bj20140614; RA Maneiro M., Peon A., Lence E., Otero J.M., Van Raaij M.J., Thompson P., RA Hawkins A.R., Gonzalez-Bello C.; RT "Insights into substrate binding and catalysis in bacterial type I RT dehydroquinase."; RL Biochem. J. 462:415-424(2014). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, RP AND SUBUNIT. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RA Minasov G., Light S.H., Shuvalova L., Papazisi L., Anderson W.F.; RT "Crystal structure of the 3-dehydroquinate dehydratase (aroD) from RT Salmonella typhimurium LT2 with citrate bound to the active Site."; RL Submitted (JAN-2010) to the PDB data bank. RN [5] RP X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-236, RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, RP SUBUNIT, MUTAGENESIS OF SER-232 AND GLN-236, AND REACTION MECHANISM. RX PubMed=21291284; DOI=10.1021/bi102020s; RA Light S.H., Minasov G., Shuvalova L., Peterson S.N., Caffrey M., RA Anderson W.F., Lavie A.; RT "A conserved surface loop in type I dehydroquinate dehydratases positions RT an active site arginine and functions in substrate binding."; RL Biochemistry 50:2357-2363(2011). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE AND MUTANT MET-170 IN RP COMPLEX WITH 3-DEHYDROQUINIC ACID, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF RP LYS-170, AND REACTION MECHANISM. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=21087925; DOI=10.1074/jbc.m110.192831; RA Light S.H., Minasov G., Shuvalova L., Duban M.E., Caffrey M., RA Anderson W.F., Lavie A.; RT "Insights into the mechanism of type I dehydroquinate dehydratases from RT structures of reaction intermediates."; RL J. Biol. Chem. 286:3531-3539(2011). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, RP AND SUBUNIT. RA Light S.H., Minasov G., Duban M.-E., Halavaty A.S., Krishna S.N., RA Shuvalova L., Kwon K., Anderson W.F.; RT "Crystal structure of the 3-dehydroquinate dehydratase (aroD) from RT Salmonella enterica typhimurium LT2 with malonate and boric acid at the RT active site."; RL Submitted (MAY-2011) to the PDB data bank. RN [8] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, RP AND SUBUNIT. RA Light S.H., Minasov G., Krishna S.N., Shuvalova L., Kwon K., Lavie A., RA Anderson W.F.; RT "1.8 angstrom crystal structure of the 3-dehydroquinate dehydratase (aroD) RT from Salmonella typhimurium LT2 with nickel bound at active site."; RL Submitted (AUG-2012) to the PDB data bank. RN [9] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANT ALA-86 IN COMPLEX WITH RP SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, MUTAGENESIS OF GLU-86, ACTIVE SITE, SUBUNIT, AND REACTION RP MECHANISM. RX PubMed=23341204; DOI=10.1002/pro.2218; RA Light S.H., Anderson W.F., Lavie A.; RT "Reassessing the type I dehydroquinate dehydratase catalytic triad: kinetic RT and structural studies of Glu86 mutants."; RL Protein Sci. 22:418-424(2013). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) WILD-TYPE AND MUTANT MET-170 IN RP COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF LYS-170, AND SUBUNIT. RX PubMed=24437575; DOI=10.1021/bi4015506; RA Light S.H., Antanasijevic A., Krishna S.N., Caffrey M., Anderson W.F., RA Lavie A.; RT "Crystal structures of type I dehydroquinate dehydratase in complex with RT quinate and shikimate suggest a novel mechanism of Schiff base formation."; RL Biochemistry 53:872-880(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. The reaction CC involves the formation of an imine intermediate between the keto group CC of 3-dehydroquinate and the epsilon-amino group of a Lys-170 at the CC active site. {ECO:0000255|HAMAP-Rule:MF_00214, CC ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:21291284, CC ECO:0000269|PubMed:23341204, ECO:0000269|PubMed:24957267}. 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:0000255|HAMAP- CC Rule:MF_00214, ECO:0000269|PubMed:21087925, CC ECO:0000269|PubMed:21291284, ECO:0000269|PubMed:23341204, CC ECO:0000269|PubMed:24957267}; CC -!- ACTIVITY REGULATION: Inhibited by (2R)-2-methyl-3-dehydroquinic acid. CC {ECO:0000269|PubMed:24957267}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=18 uM for 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius) CC {ECO:0000269|PubMed:24957267}; CC KM=21 uM for 3-dehydroquinate (at pH 7.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:21087925}; CC KM=53 uM for 3-dehydroquinate (at pH 7.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:23341204}; CC Note=kcat is 210 sec(-1) for dehydratase activity with CC 3-dehydroquinate (at pH 7.5 and 37 degrees Celsius). kcat is 255 CC sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7.2 and CC 25 degrees Celsius). kcat is 310 sec(-1) for dehydratase activity CC with 3-dehydroquinate (at pH 7.5 and 37 degrees Celsius). CC {ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:21291284, CC ECO:0000269|PubMed:23341204, ECO:0000269|PubMed:24957267}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 3/7. {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00214, CC ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:21291284, CC ECO:0000269|PubMed:23341204, ECO:0000269|PubMed:24437575, CC ECO:0000269|Ref.4, ECO:0000269|Ref.7, ECO:0000269|Ref.8}. CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family. CC {ECO:0000255|HAMAP-Rule:MF_00214}. 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; AE006468; AAL20283.1; -; Genomic_DNA. DR RefSeq; NP_460324.1; NC_003197.2. DR RefSeq; WP_000860225.1; NC_003197.2. DR PDB; 3L2I; X-ray; 1.85 A; A/B=1-252. DR PDB; 3LB0; X-ray; 1.65 A; A/B=1-252. DR PDB; 3M7W; X-ray; 1.95 A; A/B/C/D/E/F=1-252. DR PDB; 3NNT; X-ray; 1.60 A; A/B=1-252. DR PDB; 3O1N; X-ray; 1.03 A; A/B=1-252. DR PDB; 3OEX; X-ray; 1.90 A; A/B/C/D=1-252. DR PDB; 3S42; X-ray; 1.45 A; A/B=1-252. DR PDB; 4GFS; X-ray; 1.80 A; A/B=1-252. DR PDB; 4GUF; X-ray; 1.50 A; A/B=1-252. DR PDB; 4GUG; X-ray; 1.62 A; A/B=1-252. DR PDB; 4GUH; X-ray; 1.95 A; A/B=1-252. DR PDB; 4GUI; X-ray; 1.78 A; A/B=1-252. DR PDB; 4GUJ; X-ray; 1.50 A; A/B=1-252. DR PDB; 4IUO; X-ray; 1.80 A; A/B=1-252. DR PDBsum; 3L2I; -. DR PDBsum; 3LB0; -. DR PDBsum; 3M7W; -. DR PDBsum; 3NNT; -. DR PDBsum; 3O1N; -. DR PDBsum; 3OEX; -. DR PDBsum; 3S42; -. DR PDBsum; 4GFS; -. DR PDBsum; 4GUF; -. DR PDBsum; 4GUG; -. DR PDBsum; 4GUH; -. DR PDBsum; 4GUI; -. DR PDBsum; 4GUJ; -. DR PDBsum; 4IUO; -. DR AlphaFoldDB; P58687; -. DR SMR; P58687; -. DR STRING; 99287.STM1358; -. DR PaxDb; 99287-STM1358; -. DR GeneID; 1252876; -. DR KEGG; stm:STM1358; -. DR PATRIC; fig|99287.12.peg.1442; -. DR HOGENOM; CLU_064444_0_0_6; -. DR OMA; ATMAMGE; -. DR PhylomeDB; P58687; -. DR BioCyc; SENT99287:STM1358-MONOMER; -. DR BRENDA; 4.2.1.10; 2169. DR UniPathway; UPA00053; UER00086. DR EvolutionaryTrace; P58687; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IDA:UniProtKB. DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IDA:UniProtKB. 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; Aldolase class I; 1. DR HAMAP; MF_00214; AroD; 1. DR InterPro; IPR018508; 3-dehydroquinate_DH_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001381; DHquinase_I. DR NCBIfam; TIGR01093; aroD; 1. DR PANTHER; PTHR43699; 3-DEHYDROQUINATE DEHYDRATASE; 1. DR PANTHER; PTHR43699:SF1; 3-DEHYDROQUINATE DEHYDRATASE; 1. DR Pfam; PF01487; DHquinase_I; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS01028; DEHYDROQUINASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Lyase; Reference proteome; Schiff base. FT CHAIN 1..252 FT /note="3-dehydroquinate dehydratase" FT /id="PRO_0000138806" FT ACT_SITE 143 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214, FT ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, FT ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, FT ECO:0000269|Ref.8" FT ACT_SITE 170 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214, FT ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, FT ECO:0000269|Ref.4, ECO:0000269|Ref.7, ECO:0000269|Ref.8" FT BINDING 21 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214, FT ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:24437575, FT ECO:0000269|Ref.4, ECO:0000269|Ref.7" FT BINDING 46..48 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214, FT ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, FT ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, FT ECO:0000269|Ref.7" FT BINDING 82 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214, FT ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, FT ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, FT ECO:0000269|Ref.7, ECO:0000269|Ref.8" FT BINDING 213 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214, FT ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, FT ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, FT ECO:0000269|Ref.7" FT BINDING 232 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214, FT ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:24437575, FT ECO:0000269|Ref.4" FT BINDING 236 FT /ligand="3-dehydroquinate" FT /ligand_id="ChEBI:CHEBI:32364" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214, FT ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, FT ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, FT ECO:0000269|Ref.7" FT MUTAGEN 86 FT /note="E->A: Very strong reduction of the catalytic FT efficiency and almost the same affinity for FT 3-dehydroquinate." FT /evidence="ECO:0000269|PubMed:23341204" FT MUTAGEN 86 FT /note="E->Q: Strong reduction of the catalytic efficiency FT and slight increase of the affinity for 3-dehydroquinate." FT /evidence="ECO:0000269|PubMed:23341204" FT MUTAGEN 170 FT /note="K->M: Abolishes enzyme activity and 1.5-fold FT reduction of the affinity for 3-dehydroquinate." FT /evidence="ECO:0000269|PubMed:21087925, FT ECO:0000269|PubMed:24437575" FT MUTAGEN 232 FT /note="S->A: Reduces enzyme activity 50-fold." FT /evidence="ECO:0000269|PubMed:21291284" FT MUTAGEN 236 FT /note="Q->A: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:21291284" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 17..22 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 27..37 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:3O1N" FT TURN 53..56 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 58..71 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 94..107 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 121..133 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 137..146 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 167..173 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 178..194 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 207..210 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 211..214 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:3O1N" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:3O1N" FT HELIX 239..251 FT /evidence="ECO:0007829|PDB:3O1N" SQ SEQUENCE 252 AA; 27325 MW; 10BB561E38EA0A75 CRC64; MKTVTVRDLV VGEGAPKIIV SLMGKTITDV KSEALAYREA DFDILEWRVD HFANVTTAES VLEAAGAIRE IITDKPLLFT FRSAKEGGEQ ALTTGQYIDL NRAAVDSGLV DMIDLELFTG DDEVKATVGY AHQHNVAVIM SNHDFHKTPA AEEIVQRLRK MQELGADIPK IAVMPQTKAD VLTLLTATVE MQERYADRPI ITMSMSKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVA DLRTVLTILH QA //