ID   A0A3A5LQN3_STAAU        Unreviewed;       354 AA.
AC   A0A3A5LQN3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   26-FEB-2020, entry version 12.
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}, SAKG03_13740
GN   {ECO:0000313|EMBL:BBJ12736.1};
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., 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|EMBL:BBJ12736.1, ECO:0000313|Proteomes:UP000326733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KG-03 {ECO:0000313|EMBL:BBJ12736.1,
RC   ECO:0000313|Proteomes:UP000326733};
RX   PubMed=31474962;
RA   Kuroda M., Sekizuka T., Matsui H., Ohsuga J., Ohshima T., Hanaki H.;
RT   "IS256-Mediated Overexpression of the WalKR Two-Component System Regulon
RT   Contributes to Reduced Vancomycin Susceptibility in a Staphylococcus aureus
RT   Clinical Isolate.";
RL   Front. Microbiol. 10:1882-1882(2019).
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, 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, ChEBI:CHEBI:32364,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00110,
CC         ECO:0000256|SAAS:SAAS01116881};
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|HAMAP-Rule:MF_00110,
CC         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 biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       2/7. {ECO:0000256|HAMAP-Rule:MF_00110, 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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}.
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DR   EMBL; AP019542; BBJ12736.1; -; Genomic_DNA.
DR   EMBL; BDVT01000001; GBV19341.1; -; Genomic_DNA.
DR   RefSeq; WP_000776312.1; NZ_WBHU01000003.1.
DR   KEGG; saud:CH52_11745; -.
DR   KO; K01735; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000265645; Unassembled WGS sequence.
DR   Proteomes; UP000326733; 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: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, ECO:0000256|SAAS:SAAS00415284};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00415252};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00110, 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   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
//