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AROB_STAEQ
ID   AROB_STAEQ              Reviewed;         354 AA.
AC   Q5HP78;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110};
DE            Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110};
DE            EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110};
GN   Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110}; OrderedLocusNames=SERP1035;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC       7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00110};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC       Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC       or Zn(2+). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC       Dehydroquinate synthase family. {ECO:0000255|HAMAP-Rule:MF_00110}.
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DR   EMBL; CP000029; AAW54426.1; -; Genomic_DNA.
DR   RefSeq; WP_001831320.1; NC_002976.3.
DR   AlphaFoldDB; Q5HP78; -.
DR   SMR; Q5HP78; -.
DR   STRING; 176279.SERP1035; -.
DR   PRIDE; Q5HP78; -.
DR   EnsemblBacteria; AAW54426; AAW54426; SERP1035.
DR   GeneID; 50018724; -.
DR   KEGG; ser:SERP1035; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_1_9; -.
DR   OMA; IKMAVCF; -.
DR   OrthoDB; 1677032at2; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000000531; 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: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; Aromatic amino acid biosynthesis; Cobalt;
KW   Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..354
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_0000140786"
FT   BINDING         66..71
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         100..104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         124..125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         136
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         163..166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
SQ   SEQUENCE   354 AA;  40555 MW;  E29A628AB52D4606 CRC64;
     MELKTSYASD NYPIIVKHHA INSLERYIKN EEQRFFIIDK QVYNLFVDKL EALAQKFDAK
     CIVIPSGETS KSFEHYHRTI EYLLSHQLTR QTCIVAIGGG ATGDFAGFIA ATLLRGVSFV
     QVPTTILAHD SSVGGKVGIN SEHGKNLIGA FYRPKAVIYD LDFLETLPYS EILSGYAEVY
     KHALLNGEKS TKNIESNFTS NKVLQALKNL DYYLFEGIKT KLNIVVEDEK EKGKRKFLNL
     GHTFGHAIEY EHKIPHGHAV MIGILYQFIV ANHLFETNYN IQHYINYMKK LKYPLSIIKQ
     LHFEDTYHFM LLDKKNDYNG IQMVLLKNLG KPVVTHVDKD TLLSAFEELQ SYFK
 
 
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