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 27-NOV-2024, entry version 36. DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684, ECO:0000256|HAMAP-Rule:MF_00110}; DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110}; DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031, ECO:0000256|HAMAP-Rule:MF_00110}; GN Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110, GN ECO:0000313|EMBL:CAC8215039.1}; GN ORFNames=DQU50_03500 {ECO:0000313|EMBL:TXL46896.1}, DQU51_15755 GN {ECO:0000313|EMBL:TXL38908.1}, G6Y24_13150 GN {ECO:0000313|EMBL:NGW68405.1}, GZ111_000905 GN {ECO:0000313|EMBL:XAJ30604.1}, M1K003_0309 GN {ECO:0000313|EMBL:GBV19341.1}, SAMEA70153168_00398 GN {ECO:0000313|EMBL:CAC8215039.1}; OS Staphylococcus aureus. OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280 {ECO:0000313|EMBL:NGW68405.1, ECO:0000313|Proteomes:UP000473113}; RN [1] {ECO:0000313|Proteomes:UP000265645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1K003 {ECO:0000313|Proteomes:UP000265645}; RA Nakamura Y., Takahashi H., Takaya A., Inoue Y., Katayama Y., Kusuya Y., RA Shoji T., Takada S., Nakagawa S., Oguma R., Ozawa N., Yamaide F., RA Suzuki S., Villaruz A., Otto M., Matsue H., Nunez G., Shimojo N.; RT "Protection against atopic dermatitis through acquisition of Staphylococcus RT quorum-sensing agr mutations in the skin."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000451682, ECO:0000313|Proteomes:UP000488373} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=pt013 {ECO:0000313|Proteomes:UP000451682}, Pt013 RC {ECO:0000313|EMBL:TXL46896.1}, pt014 RC {ECO:0000313|Proteomes:UP000488373}, and Pt014 RC {ECO:0000313|EMBL:TXL38908.1}; RA Sullivan M.J., Altman D.R., Chacko K., Ciferri B., Webster E., Deikus G., RA Lewis M., Khan Z., Beckford C., Rendo A., Samaroo F., Sebra R., RA Karam-Howlin R., Southwick K., Adams E., Ying L., Kornblum J., Factor S., RA Danesh Yazdi M., Dingle T., Hamula C., Bashir A., Schadt E., Kasarskis A., RA Patel G., Wallach F., Gibbs K., Van Bakel H.; RT "Whole genome sequencing to identify and define MRSA outbreaks."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:GBV19341.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1K003 {ECO:0000313|EMBL:GBV19341.1}; RA Nakamura Y., Takahashi H., Takaya A., Inoue Y., Katayama Y., Kusuya Y., RA Shoji T., Takada S., Nakagawa S., Oguma R., Ozawa N., Yamaide F., RA Suzuki S., Villaruz A., Otto M., Matsue H., Nunez G., Shimojo N.; RT "Protection against atopic dermatitis through acquisition of Staphylococcus RT quorum-sensing agr mutations in the skin."; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {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 [5] {ECO:0000313|EMBL:CAC8215039.1, ECO:0000313|Proteomes:UP000507402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MOS114 {ECO:0000313|EMBL:CAC8215039.1, RC ECO:0000313|Proteomes:UP000507402}; RG Pathogen Informatics; RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:XAJ30604.1, ECO:0000313|Proteomes:UP000461227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17-021 {ECO:0000313|EMBL:XAJ30604.1, RC ECO:0000313|Proteomes:UP000461227}; RX PubMed=34346711; RA Little S.V., Hillhouse A.E., Lawhon S.D., Bryan L.K.; RT "Analysis of Virulence and Antimicrobial Resistance Gene Carriage in RT Staphylococcus aureus Infections in Equids Using Whole-Genome Sequencing."; RL MSphere 6:e0019620-e0019620(2021). RN [7] {ECO:0000313|EMBL:XAJ30604.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=17-021 {ECO:0000313|EMBL:XAJ30604.1}; RA Bryan L.K.; RL Submitted (APR-2024) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate CC 7-phosphate (DAHP) to dehydroquinate (DHQ). CC {ECO:0000256|ARBA:ARBA00003485, ECO:0000256|HAMAP-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|ARBA:ARBA00001393, ECO:0000256|HAMAP- CC 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|ARBA:ARBA00004661, ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. CC Dehydroquinate synthase family. {ECO:0000256|ARBA:ARBA00005412, CC 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; CAIIGN010000001; CAC8215039.1; -; Genomic_DNA. DR EMBL; BDVT01000001; GBV19341.1; -; Genomic_DNA. DR EMBL; JAALTR010000315; NGW68405.1; -; Genomic_DNA. DR EMBL; QNXH01000001; TXL38908.1; -; Genomic_DNA. DR EMBL; QNXF01000002; TXL46896.1; -; Genomic_DNA. DR EMBL; CP152420; XAJ30604.1; -; Genomic_DNA. DR RefSeq; WP_000776312.1; NZ_WYCZ01000002.1. DR KEGG; saud:CH52_11745; -. DR OMA; TGINTPY; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000265645; Unassembled WGS sequence. DR Proteomes; UP000451682; Unassembled WGS sequence. DR Proteomes; UP000461227; Chromosome. DR Proteomes; UP000473113; Unassembled WGS sequence. DR Proteomes; UP000488373; Unassembled WGS sequence. DR Proteomes; UP000507402; 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-KW. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.50.1970:FF:000019; 3-dehydroquinate synthase; 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. 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00110}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_00110}; KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_00110}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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 //