ID   A0A3A5LQN3_STAAU        Unreviewed;       354 AA.
AC   A0A3A5LQN3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   13-FEB-2019, entry version 3.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210916};
DE            Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
DE            EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210941};
GN   Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110,
GN   ECO:0000313|EMBL:GBV19341.1};
GN   ORFNames=D5R87_08095 {ECO:0000313|EMBL:RJT61195.1}, D5R88_13345
GN   {ECO:0000313|EMBL:RJT70085.1}, M1K003_0309
GN   {ECO:0000313|EMBL:GBV19341.1};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:RJT61195.1};
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.
RN   [2] {ECO:0000313|EMBL:RJT61195.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SABHZ053 {ECO:0000313|EMBL:RJT61195.1};
RA   Tang B., Zhang L., Chang J., Luo Y.;
RT   "Genome sequencing of Staphylococcus aureus strain SABHZ053.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:RJT70085.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SABHZ079 {ECO:0000313|EMBL:RJT70085.1};
RA   Tang B., Zhang L., Chang J., Luo Y.;
RT   "Genome sequencing of Staphylococcus aureus strain SABHZ079.";
RL   Submitted (SEP-2018) 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:SAAS00210934}.
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:RJT61195.1}.
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DR   EMBL; BDVT01000001; GBV19341.1; -; Genomic_DNA.
DR   EMBL; QZVV01000009; RJT61195.1; -; Genomic_DNA.
DR   EMBL; QZVW01000026; RJT70085.1; -; Genomic_DNA.
DR   RefSeq; WP_000776312.1; NZ_UHBV01000001.1.
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:SAAS00210890};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS00210867};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS00210864};
KW   Complete proteome {ECO:0000313|Proteomes:UP000265645};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS00210856};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00958949,
KW   ECO:0000313|EMBL:RJT61195.1};
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:SAAS00210880};
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:SAAS00210870}.
FT   DOMAIN       62    316       DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
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
//