ID AROB_BUCAI Reviewed; 363 AA. AC P57604; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 129. 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}; OrderedLocusNames=BU538; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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; BA000003; BAB13231.1; -; Genomic_DNA. DR RefSeq; NP_240345.1; NC_002528.1. DR RefSeq; WP_009874489.1; NC_002528.1. DR AlphaFoldDB; P57604; -. DR SMR; P57604; -. DR STRING; 563178.BUAP5A_531; -. DR EnsemblBacteria; BAB13231; BAB13231; BAB13231. DR KEGG; buc:BU538; -. DR PATRIC; fig|107806.10.peg.543; -. DR eggNOG; COG0337; Bacteria. DR HOGENOM; CLU_001201_0_2_6; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000001806; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. 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; cd08195; DHQS; 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; IPR016037; DHQ_synth_AroB. DR InterPro; IPR030963; DHQ_synth_fam. DR InterPro; IPR030960; DHQS/DOIS. 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 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..363 FT /note="3-dehydroquinate synthase" FT /id="PRO_0000140717" FT BINDING 74..79 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 108..112 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 132..133 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 145 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 154 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 172..175 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 187 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 250 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 267 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" SQ SEQUENCE 363 AA; 40297 MW; 1DB8EC7B8D8F6EC8 CRC64; MKIVERLQVV LGERSYPISI GAGIIQEDDI FWPLKPGDQA MLVTNKTLAN LLKDKVFYHL RKSGIKIDQV ILSDGEQYKT LNEMELIISA LLEKKHARDT TLIALGGGVI GDLAGFAASV YQRGVRFIQI PTTLLSQVDA SVGGKTAVNH LLGKNMIGSF WQPSSVIIDI DCLKTLPYNE LVSGMAEVIK YAIVFDKTFF CWLEENIESI LSLNHTAMSY CIKKCCELKS QLIALDEREN NLRALLNLGH TYGHAIEVHA GYGNWLHGEA ISVGMVMAAR TSELLGHLKT IDFKRILVLL KRTGLPIKGP KNMSAASYLP YMMRDKKVIS GEMRLVLPLS IGKAEIYSNI DKNIILTAIK HSQ //