ID A0A3A5LQN3_STAAU Unreviewed; 354 AA. AC A0A3A5LQN3; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 18-SEP-2019, entry version 8. DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00336730}; DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110}; DE EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00336723}; GN Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110, GN ECO:0000313|EMBL:GBV19341.1}; GN ORFNames=M1K003_0309 {ECO:0000313|EMBL:GBV19341.1}; OS Staphylococcus aureus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280 {ECO:0000313|EMBL:GBV19341.1, ECO:0000313|Proteomes:UP000265645}; RN [1] {ECO:0000313|EMBL:GBV19341.1, ECO:0000313|Proteomes:UP000265645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1K003 {ECO:0000313|EMBL:GBV19341.1, RC ECO:0000313|Proteomes:UP000265645}; RA Nakamura Y., Takahashi H., Takaya A., Inoue Y., Katayama Y., RA Kusuya Y., Shoji T., Takada S., Nakagawa S., Oguma R., Ozawa N., RA Yamaide F., Suzuki S., Villaruz A., Otto M., Matsue H., Nunez G., RA Shimojo N.; RT "Protection against atopic dermatitis through acquisition of RT Staphylococcus quorum-sensing agr mutations in the skin."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino- CC heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). CC {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00858858}. CC -!- CATALYTIC ACTIVITY: CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3- CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, CC ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; CC EC=4.2.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00110, CC ECO:0000256|SAAS:SAAS01116881}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00110}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00110}; CC Note=Binds 1 divalent metal cation per subunit. Can use either CC Co(2+) or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00110, ECO:0000256|SAAS:SAAS00336779}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|SAAS:SAAS00607009}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_00110, CC ECO:0000256|SAAS:SAAS00210851}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110, CC ECO:0000256|SAAS:SAAS00336740}. CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. CC Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110, CC ECO:0000256|SAAS:SAAS00858850}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GBV19341.1}. 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; BDVT01000001; GBV19341.1; -; Genomic_DNA. DR RefSeq; WP_000776312.1; NZ_UHCK01000001.1. DR SMR; A0A3A5LQN3; -. DR KEGG; saud:CH52_11745; -. DR KO; K01735; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000265645; 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: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 ECO:0000256|SAAS:SAAS00415276}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00415253}; KW Cobalt {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00415284}; KW Complete proteome {ECO:0000313|Proteomes:UP000265645}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00415252}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00958949}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS01080055}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00415338}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00858852}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210932}. FT NP_BIND 100 104 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}. FT NP_BIND 124 125 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}. FT NP_BIND 163 166 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}. FT METAL 178 178 Cobalt or zinc. {ECO:0000256|HAMAP-Rule: FT MF_00110}. FT METAL 242 242 Cobalt or zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00110}. FT METAL 256 256 Cobalt or zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00110}. FT BINDING 136 136 NAD; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00110}. FT BINDING 145 145 NAD. {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 //