ID AROB_LISMH Reviewed; 365 AA. AC B8DBZ9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 02-SEP-2026, entry version 78. DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110}; DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110}; DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110}; GN Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110}; GN OrderedLocusNames=LMHCC_0629; OS Listeria monocytogenes serotype 4a (strain HCC23). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Listeriaceae; OC Listeria. OX NCBI_TaxID=552536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HCC23; RX PubMed=21602330; DOI=10.1128/jb.05236-11; RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M., RA Lawrence M.L.; RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23."; RL J. Bacteriol. 193:3679-3680(2011). CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP- CC Rule:MF_00110}. CC -!- CATALYTIC ACTIVITY: CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3- CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00110}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00110}; CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+) CC or Zn(2+). {ECO:0000255|HAMAP-Rule:MF_00110}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00110}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 2/7. {ECO:0000255|HAMAP-Rule:MF_00110}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}. CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. CC Dehydroquinate synthase family. {ECO:0000255|HAMAP-Rule:MF_00110}. 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; CP001175; ACK38985.1; -; Genomic_DNA. DR RefSeq; WP_012581062.1; NC_011660.1. DR AlphaFoldDB; B8DBZ9; -. DR SMR; B8DBZ9; -. DR KEGG; lmh:LMHCC_0629; -. DR HOGENOM; CLU_001201_0_1_9; -. DR UniPathway; UPA00053; UER00085. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd08195; DHQS; 1. DR FunFam; 1.20.1090.10:FF:000019; 3-dehydroquinate synthase; 1. DR FunFam; 3.40.50.1970:FF:000026; 3-dehydroquinate synthase; 1. DR Gene3D; 3.40.50.1970; -; 1. DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1. DR HAMAP; MF_00110; DHQ_synthase; 1. DR InterPro; IPR050071; Dehydroquinate_synthase. DR InterPro; IPR016037; DHQ_synth_AroB. DR InterPro; IPR030963; DHQ_synth_fam. DR InterPro; IPR030960; DHQS/DOIS_N. DR InterPro; IPR056179; DHQS_C. DR NCBIfam; TIGR01357; aroB; 1. DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1. DR PANTHER; PTHR43622:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 1. DR Pfam; PF01761; DHQ_synthase; 1. DR Pfam; PF24621; DHQS_C; 1. DR PIRSF; PIRSF001455; DHQ_synth; 1. DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt; KW Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding; Zinc. FT CHAIN 1..365 FT /note="3-dehydroquinate synthase" FT /id="PRO_1000119084" FT BINDING 106..110 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 130..131 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 142 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 151 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 169..172 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 184 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 264 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" SQ SEQUENCE 365 AA; 41142 MW; DBDB87B00F5A4CCA CRC64; MPEITVRAKS KTYPVYINEF ALEDVREKWT ESLAKFSHVF VLTDEHVAEL HKAKLDAVLA DLPVVTYYVA PNGEEAKTFR VYEDVMTKLI ETGLDRKAVL IAFGGGVIGD LGGFVAATYM RGIPFYQVPT TVLAHDSAVG GKVAINHPLG KNMIGNFYQP EAVIYDTQFF ATLPEREMRS GFAEMIKHAL ISDQTLLRAL MDTFTEPKDF YTKDLTPFLQ RGIEIKANIV AQDETEQGVR AYLNFGHTFG HALEAYGNFG KWLHGEAITY GMIYALTMSE AIYGLDFDLA EFKTWLKQLG YDTTFDATVP FSKILENMRH DKKTTFNEIS MVLLEEIGKP VIFKAEDDLI FETYKRVMRN GGNGI //