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AROB_NEIG1
ID   AROB_NEIG1              Reviewed;         359 AA.
AC   Q5FAD4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=NGO0092;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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: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=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   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={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; AE004969; AAW88853.1; -; Genomic_DNA.
DR   RefSeq; WP_003690567.1; NC_002946.2.
DR   RefSeq; YP_207265.1; NC_002946.2.
DR   AlphaFoldDB; Q5FAD4; -.
DR   SMR; Q5FAD4; -.
DR   STRING; 242231.NGO_0092; -.
DR   EnsemblBacteria; AAW88853; AAW88853; NGO_0092.
DR   GeneID; 66752358; -.
DR   KEGG; ngo:NGO_0092; -.
DR   PATRIC; fig|242231.10.peg.120; -.
DR   HOGENOM; CLU_001201_0_2_4; -.
DR   OMA; YGVIWDA; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000000535; 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..359
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_0000231100"
FT   BINDING         71..76
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         105..109
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         129..130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         142
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         151
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         169..172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
SQ   SEQUENCE   359 AA;  38581 MW;  BE705DB9B44DEDBE CRC64;
     MKTLTVHTPS HSYPIFIGNG LLPQAGSLLK PHLGKRAAII TNETVAPLYL GTLQTALDAA
     GVSHFSIILP DGEAHKNWQT LNLIFDGLMQ NRAERKTTLI ALGGGVIGDM VGFAAATYQR
     GAPFIQIPTT LLSQVDSSVG GKTAINHPLG KNMIGAFYQP QAVLADLDTL HTLPARELSA
     GMAEVIKYGA LGDIGFFEWL EQHMPELMAL ERAPLTQAVY RCCQMKADIV AQDETEQGIR
     AWLNLGHTFG HAVEAEMGYG VWLHGEAVAA GCVLAARLSE QLGKTSAADT ARLAALLEAA
     GLPSAPPVFA FEKWLAHMSH DKKVSGGIMR FIGLNRLGEA VITEITDTDI LRRTLQPYL
 
 
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