ID   AROB_PROM1              Reviewed;         368 AA.
AC   A2C1E0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=NATL1_07421;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000553; ABM75300.1; -; Genomic_DNA.
DR   RefSeq; WP_011823456.1; NC_008819.1.
DR   AlphaFoldDB; A2C1E0; -.
DR   SMR; A2C1E0; -.
DR   STRING; 167555.NATL1_07421; -.
DR   EnsemblBacteria; ABM75300; ABM75300; NATL1_07421.
DR   KEGG; pme:NATL1_07421; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_2_3; -.
DR   OMA; YGVIWDA; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000002592; 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..368
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_1000094561"
FT   BINDING         112..116
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         136..137
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         191
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"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
SQ   SEQUENCE   368 AA;  40601 MW;  31D44EF2808B9EB4 CRC64;
     MNKDNHHIKV SLTNNPYEIV IGKNSLESIG DELFNIGFRE GLKVLVVSNK EVSDHYGDCI
     IKSLIKSKFK PKLLIIKAGE DQKNQSSIDL IHNAAYEARL ERGSLMIALG GGVIGDMTGF
     AAATWLRGVN VVQIPTTLLA MVDASIGGKT GINHSKGKNL IGAFHQPRLV LIDPKTLISL
     PSREFKAGMA EIIKYGVISD LELFDLLERQ ENIADLSNIK EKLLLEIIKR SAKSKAEIVI
     KDEKESGVRA FLNYGHTFGH VIENLCGYGK WLHGEAVAMG MVAVGQLAVQ RGLWNEDNAK
     RQKRLIEKAG LPSNWPKLDI ESVLSSLQGD KKVKNGKVSF VMPLKIGDVK LFNNISNKEI
     RECLQKIS