ID AROB_SYNY3 Reviewed; 361 AA. AC P73997; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 160. 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=slr2130; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Merismopediaceae; Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000255|HAMAP- CC 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 -!- 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 ECO:0000305}. 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; BA000022; BAA18068.1; -; Genomic_DNA. DR PIR; S75507; S75507. DR AlphaFoldDB; P73997; -. DR SMR; P73997; -. DR FunCoup; P73997; 436. DR IntAct; P73997; 5. DR STRING; 1148.gene:10498939; -. DR PaxDb; 1148-gene:10498939; -. DR EnsemblBacteria; BAA18068; BAA18068; BAA18068. DR KEGG; syn:slr2130; -. DR eggNOG; COG0337; Bacteria. DR InParanoid; P73997; -. DR PhylomeDB; P73997; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd08195; DHQS; 1. DR FunFam; 1.20.1090.10:FF:000040; 3-dehydroquinate synthase; 1. DR FunFam; 3.40.50.1970:FF:000007; Pentafunctional AROM polypeptide; 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; KW Reference proteome; Zinc. FT CHAIN 1..361 FT /note="3-dehydroquinate synthase" FT /id="PRO_0000140800" FT BINDING 107..111 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 131..132 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 144 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 153 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 251 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 268 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" SQ SEQUENCE 361 AA; 38855 MW; D7EC4CEE741486BC CRC64; MATTIPVPLP QSPYQVQIVP GGLAAIADHL APLGLGKKIM VVSNPEIYDY YGEVVIQALQ RAGYEVFQHL IPAGETHKTL ASINELYDVA FQANLERNST LLSLGGGVIG DMTGFGAATW LRGINFVQVP TSLLAMVDAS IGGKTGVNHP QGKNLIGAFY QPRLVYIDPV VLKTLPEREF RAGMAEVIKY GVIWDSELFT ALEEAEDLSS IDRLPDELLT KIIQRSCQAK VDVVSQDEKE AGLRAILNYG HTVGHGVESL TGYGVINHGE AVAIGMEAAA KIAHYLGLCD QSLGDRQRQL LLKTKLPTEM PPTLAVENLL ASLLHDKKVK AGKVRFILPT AIGQVTISDA VTDEVIKATL G //