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 29-SEP-2021, entry version 21. 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 ECO:0000313|EMBL:CAC6438418.1}; GN ORFNames=BSG37_07765 {ECO:0000313|EMBL:APZ40288.1}, E5491_07685 GN {ECO:0000313|EMBL:QBZ85664.1}, FAF32_010635 GN {ECO:0000313|EMBL:TXD26079.1}, G6X35_10705 GN {ECO:0000313|EMBL:NGV91864.1}, G6X37_05040 GN {ECO:0000313|EMBL:NGS81730.1}, G6Y24_13150 GN {ECO:0000313|EMBL:NGW68405.1}, GO810_08255 GN {ECO:0000313|EMBL:MVK38039.1}, SAMEA103891454_01922 GN {ECO:0000313|EMBL:CAC6438418.1}; OS Staphylococcus aureus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280 {ECO:0000313|EMBL:QBZ85664.1, ECO:0000313|Proteomes:UP000296718}; RN [1] {ECO:0000313|EMBL:APZ40288.1, ECO:0000313|Proteomes:UP000187007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCI 28 {ECO:0000313|EMBL:APZ40288.1, RC ECO:0000313|Proteomes:UP000187007}; RA Nicholson T.L., Bayles D.O., Hau S.J.; RT "Staphylococcus aureus UCI 28 MRSA ST5."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QBZ85664.1, ECO:0000313|Proteomes:UP000296718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCUH29 {ECO:0000313|EMBL:QBZ85664.1, RC ECO:0000313|Proteomes:UP000296718}; RA Silverstein K., Yang J.; RT "Complete Genome Sequence of the Hospital-Acquired Methicillin-Resistant RT Staphylococcus aureus Strain WCUH29."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:QBZ85664.1, ECO:0000313|Proteomes:UP000296718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCUH29 {ECO:0000313|EMBL:QBZ85664.1, RC ECO:0000313|Proteomes:UP000296718}; RA Ji Y., Lei T., Zhang Y.; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:TXD26079.1, ECO:0000313|Proteomes:UP000307619} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=14 {ECO:0000313|EMBL:TXD26079.1, RC ECO:0000313|Proteomes:UP000307619}; RA Fouts D., Sutton G., Singh I., Kevin A.; RT "WGS of SAMN11458148."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:MVK38039.1, ECO:0000313|Proteomes:UP000432480} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S_3030.LEPB.AN {ECO:0000313|EMBL:MVK38039.1, RC ECO:0000313|Proteomes:UP000432480}; RA Stine O.C.; RT "Implementation of targeted gown and glove precautions to prevent RT Staphylococcus aureus acquisition in community-based nursing homes."; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|Proteomes:UP000473113, ECO:0000313|Proteomes:UP000474795} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UB561 {ECO:0000313|EMBL:NGV91864.1, RC ECO:0000313|Proteomes:UP000474795}, UB564 RC {ECO:0000313|EMBL:NGS81730.1, ECO:0000313|Proteomes:UP000480948}, and RC 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 [7] {ECO:0000313|EMBL:CAC6438418.1, ECO:0000313|Proteomes:UP000504931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRS749 {ECO:0000313|EMBL:CAC6438418.1, RC ECO:0000313|Proteomes:UP000504931}; RG Pathogen Informatics; RL Submitted (JUN-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; CP018768; APZ40288.1; -; Genomic_DNA. DR EMBL; CAIHGC010000006; CAC6438418.1; -; Genomic_DNA. DR EMBL; WPTJ01000097; MVK38039.1; -; Genomic_DNA. DR EMBL; JAALQG010000152; NGS81730.1; -; Genomic_DNA. DR EMBL; JAALTV010000370; NGV91864.1; -; Genomic_DNA. DR EMBL; JAALTR010000315; NGW68405.1; -; Genomic_DNA. DR EMBL; CP039156; QBZ85664.1; -; Genomic_DNA. DR EMBL; SULB02000042; TXD26079.1; -; Genomic_DNA. DR RefSeq; WP_000776312.1; NZ_WYDB01000002.1. DR EnsemblBacteria; GBV19341; GBV19341; M1K003_0309. DR EnsemblBacteria; QBZ85664; QBZ85664; E5491_07685. DR KEGG; saud:CH52_11745; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000187007; Chromosome. DR Proteomes; UP000296718; Chromosome. DR Proteomes; UP000307619; Unassembled WGS sequence. DR Proteomes; UP000432480; Unassembled WGS sequence. DR Proteomes; UP000473113; Unassembled WGS sequence. DR Proteomes; UP000474795; Unassembled WGS sequence. DR Proteomes; UP000480948; Unassembled WGS sequence. DR Proteomes; UP000504931; 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: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="Cobalt or zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT METAL 242 FT /note="Cobalt or zinc; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT METAL 256 FT /note="Cobalt or 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 //