ID A0A3A5LQN3_STAAU Unreviewed; 354 AA. AC A0A3A5LQN3; A0A4V1C9J9; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 22-FEB-2023, entry version 27. DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110}; DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110}; DE EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110}; GN Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110}; GN ORFNames=G6Y24_13150 {ECO:0000313|EMBL:NGW68405.1}; OS Staphylococcus aureus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280 {ECO:0000313|EMBL:NGW68405.1, ECO:0000313|Proteomes:UP000473113}; RN [1] {ECO:0000313|EMBL:NGW68405.1, ECO:0000313|Proteomes:UP000473113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UG255 {ECO:0000313|EMBL:NGW68405.1, RC ECO:0000313|Proteomes:UP000473113}; RA Castro-Cardozo B., Berrio M., Vargas M.L., Carvajal L.P., Millan L.V., RA Rios R., Hernandez A., Rincon S.L., Cubides P., Forero E., Dinh A., RA Seas C., Munita J.M., Arias C.A., Reyes J., Diaz L.; RT "Detection of Heterogeneous Vancomycin Intermediate Resistance in RT Methicillin Resistant Staphylococcus aureus Isolates from Latin-America."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00110}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00110}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00110}; CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+) CC or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|ARBA:ARBA00001911, CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00110}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. CC Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}. 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:NGW68405.1}. 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; JAALTR010000315; NGW68405.1; -; Genomic_DNA. DR RefSeq; WP_000776312.1; NZ_WYDB01000002.1. DR AlphaFoldDB; A0A3A5LQN3; -. DR SMR; A0A3A5LQN3; -. DR EnsemblBacteria; GBV19341; GBV19341; M1K003_0309. DR KEGG; saud:CH52_11745; -. DR OMA; IKMAVCF; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000473113; Unassembled WGS sequence. 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 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 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. DR TIGRFAMs; TIGR01357; aroB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110}; KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_00110}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00110}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00110}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00110}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00110}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}. FT DOMAIN 62..316 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000259|Pfam:PF01761" FT BINDING 100..104 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 124..125 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 136 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 145 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 163..166 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 178 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 242 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 256 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" SQ SEQUENCE 354 AA; 40237 MW; 59AB2D0C089B872D CRC64; MKLQTTYPSN NYPIFVEHGA IDHISTYIDQ FDQSFILIDE HVNQYFADKF DDILSYENVH KVIIPAGEKT KTFEQYQETL EYILSHHVTR NTAIIAVGGG ATGDFAGFVA ATLLRGVHFI QVPTTILAHD SSVGGKVGIN SKQGKNLIGA FYRPTAVIYD LDFLKTLPFE QILSGYAEVY KHALLNGEST TQEIEQHFKD REILQSLNGM DKYIAKGIET KLDIVVADEK EQGVRKFLNL GHTFGHAVEY NHKIAHGHAV MIGIIYQFIV ANILFNSNHD IQHYINYLTK LGYPLETITD IDFETIYQYM LSDKKNDKQG VQMVLIKHFG DIVVQHIDQT TLQHACEQLK TYFK //