ID   AROB_BACC2              Reviewed;         361 AA.
AC   B7IP95;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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};
GN   OrderedLocusNames=BCG9842_B3772;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) 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; CP001186; ACK93926.1; -; Genomic_DNA.
DR   RefSeq; WP_000526805.1; NC_011772.1.
DR   AlphaFoldDB; B7IP95; -.
DR   SMR; B7IP95; -.
DR   PRIDE; B7IP95; -.
DR   EnsemblBacteria; ACK93926; ACK93926; BCG9842_B3772.
DR   KEGG; bcg:BCG9842_B3772; -.
DR   HOGENOM; CLU_001201_0_2_9; -.
DR   OMA; YGVIWDA; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000006744; 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; Zinc.
FT   CHAIN           1..361
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_1000117472"
FT   BINDING         72..77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         130..131
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         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   361 AA;  40093 MW;  E3E2CED7670CFFD0 CRC64;
     MGNIHIQTKS KEYDVHVGKE ALSHLTMIVQ NMQPAVSNVM IISDEAVASL HLQTVIDALQ
     VEQDVFSFVV PSGEKEKSFE NFYAAHTSAL ENKLDRNSLI LALGGGMIGD LAGFVAASFM
     RGIRFVQVPT TLLAHDSAVG GKVAINHPLG KNMIGAFHQP EAVVYHTPFL QSLPKKEWRS
     GYAEVIKHAL IGDVELYHWL KEEVQTLADL RDEKLIHILT KAIPVKANVV SQDETEKGVR
     AHLNFGHTLG HALEKELGYG NITHGDGVAV GMLFAIFLSE QVYKVNLAYE DMKQWFLKYG
     YPKMPRDLNV ERLVQLMKQD KKANAGAIHM VLMQEYGVVN VVSISDETVH IALEAFQKDM
     V