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 25-MAY-2022, entry version 23. 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}, HK402_07185 GN {ECO:0000313|EMBL:QJR32546.1}; 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. RN [2] {ECO:0000313|EMBL:QJR32546.1, ECO:0000313|Proteomes:UP000502142} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SA01 {ECO:0000313|EMBL:QJR32546.1, RC ECO:0000313|Proteomes:UP000502142}; RA Zhu Y., Wang C., Schwarz S., Liu W., Zhang W.; RT "Analysis of a multiresistant Staphylococcus aureus strain of chicken RT origin."; RL Submitted (MAY-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 --------------------------------------------------------------------------- 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 EMBL; CP053075; QJR32546.1; -; Genomic_DNA. DR RefSeq; WP_000776312.1; NZ_WYDB01000002.1. 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 Proteomes; UP000502142; 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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. 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 Pfam; PF01761; DHQ_synthase; 1. DR PIRSF; PIRSF001455; DHQ_synth; 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="DHQ_synthase" FT /evidence="ECO:0000259|Pfam:PF01761" FT NP_BIND 100..104 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT NP_BIND 124..125 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT NP_BIND 163..166 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT METAL 178 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT METAL 242 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT METAL 256 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 136 FT /note="NAD; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 145 FT /note="NAD" 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 //