ID   DHQS_HALS3              Reviewed;         387 AA.
AC   B0R336;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_01244};
DE            Short=DHQ synthase {ECO:0000255|HAMAP-Rule:MF_01244};
DE            EC=1.4.1.24 {ECO:0000255|HAMAP-Rule:MF_01244};
DE   AltName: Full=3-dehydroquinate synthase II {ECO:0000255|HAMAP-Rule:MF_01244};
GN   Name=aroB' {ECO:0000255|HAMAP-Rule:MF_01244}; OrderedLocusNames=OE_1475F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- FUNCTION: Catalyzes the oxidative deamination and cyclization of 2-
CC       amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-
CC       dehydroquinate (DHQ), which is fed into the canonical shikimic pathway
CC       of aromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)
CC         = 3-dehydroquinate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:25956,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58859; EC=1.4.1.24; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01244};
CC   -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01244}.
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DR   EMBL; AM774415; CAP13146.1; -; Genomic_DNA.
DR   RefSeq; WP_010902185.1; NC_010364.1.
DR   AlphaFoldDB; B0R336; -.
DR   SMR; B0R336; -.
DR   EnsemblBacteria; CAP13146; CAP13146; OE_1475F.
DR   GeneID; 5952474; -.
DR   GeneID; 62886003; -.
DR   KEGG; hsl:OE_1475F; -.
DR   HOGENOM; CLU_056379_0_0_2; -.
DR   OMA; HFGMAIK; -.
DR   PhylomeDB; B0R336; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR   GO; GO:0102042; F:dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01244; Arch_DHQ_synthase; 1.
DR   InterPro; IPR002812; DHQ_synth.
DR   PANTHER; PTHR33563; PTHR33563; 1.
DR   Pfam; PF01959; DHQS; 1.
DR   PIRSF; PIRSF006655; DHQ_synth; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD;
KW   Oxidoreductase.
FT   CHAIN           1..387
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_0000372044"
SQ   SEQUENCE   387 AA;  41474 MW;  F919FFE345BE83ED CRC64;
     MTRSVWLKAD DEVGDWETRK RRITAGLEAG VDWVLVDRAD VARVRELGSV NVAAFSTDDA
     NVIEDAEGTD ADPDAYVAGK DGEGDGTVDL PADFSGSADL SALRRGHADT AYVRIRDEEY
     EPFAQAAAEV ADHTIVVGDD WTIIPLENLI ARIGEETTLV AGVESAAEAE TAFETLDIGA
     DAVLLDSDDP DEIRRTVSVR DAADREHLAL STATITTIEE AGSADRVCVD TGSLLADDEG
     MLVGSMSRGL FFVHAETAQS PYVAARPFRV NAGAVHAYVR TPDGGTKYLA ELGSGDEVQV
     VDGDGRTRSA VVGRAKIEKR PMFRVEAETD DGDRIETLLQ NAETIKVATP NGRTAVTDLS
     VGDDLHVFLQ DGGRHFGEAI DERIIEQ