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   19-JAN-2022, entry version 22.
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:CAC6453092.1};
GN   ORFNames=DQV20_10555 {ECO:0000313|EMBL:TXL52999.1}, G6X35_10705
GN   {ECO:0000313|EMBL:NGV91864.1}, G6Y24_13150
GN   {ECO:0000313|EMBL:NGW68405.1}, HK402_07185
GN   {ECO:0000313|EMBL:QJR32546.1}, SAMEA103891463_02234
GN   {ECO:0000313|EMBL:CAC6453092.1};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:NGV91864.1, ECO:0000313|Proteomes:UP000474795};
RN   [1] {ECO:0000313|EMBL:TXL52999.1, ECO:0000313|Proteomes:UP000434213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt081 {ECO:0000313|EMBL:TXL52999.1}, and pt081
RC   {ECO:0000313|Proteomes:UP000434213};
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   [2] {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}, and UG255
RC   {ECO:0000313|EMBL:NGW68405.1, 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   [3] {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.
RN   [4] {ECO:0000313|EMBL:CAC6453092.1, ECO:0000313|Proteomes:UP000505394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRS758 {ECO:0000313|EMBL:CAC6453092.1,
RC   ECO:0000313|Proteomes:UP000505394};
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}.
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DR   EMBL; CAIHGI010000008; CAC6453092.1; -; Genomic_DNA.
DR   EMBL; JAALTV010000370; NGV91864.1; -; Genomic_DNA.
DR   EMBL; JAALTR010000315; NGW68405.1; -; Genomic_DNA.
DR   EMBL; CP053075; QJR32546.1; -; Genomic_DNA.
DR   EMBL; QNXI01000001; TXL52999.1; -; Genomic_DNA.
DR   RefSeq; WP_000776312.1; NZ_WYDB01000002.1.
DR   EnsemblBacteria; GBV19341; GBV19341; M1K003_0309.
DR   KEGG; saud:CH52_11745; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000434213; Unassembled WGS sequence.
DR   Proteomes; UP000473113; Unassembled WGS sequence.
DR   Proteomes; UP000474795; Unassembled WGS sequence.
DR   Proteomes; UP000502142; Chromosome.
DR   Proteomes; UP000505394; 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="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
//