ID   DHQS_CENSY              Reviewed;         338 AA.
AC   A0RU27;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 51.
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};
GN   OrderedLocusNames=CENSYa_0201;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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; DP000238; ABK76844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RU27; -.
DR   STRING; 414004.CENSYa_0201; -.
DR   EnsemblBacteria; ABK76844; ABK76844; CENSYa_0201.
DR   KEGG; csy:CENSYa_0201; -.
DR   PATRIC; fig|414004.10.peg.176; -.
DR   HOGENOM; CLU_056379_0_0_2; -.
DR   OMA; HFGMAIK; -.
DR   Proteomes; UP000000758; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..338
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_0000372043"
SQ   SEQUENCE   338 AA;  37043 MW;  143FF962D055DCEB CRC64;
     MPRAQLQRFL SGISAEGIRT VYLDPKDAAK AKLDAMHSSP SSRYVVLEGR AAKPRGKKVG
     RRFKILSNKD IDGVLQEAQK GLDFVITEVQ DWKIIPLENM IAKLHKIHTR LYAVARSPAE
     VRKMFSILDV GVDGVIFTAS TVGDVREALV HLGTKSFRLQ PARITEIREV GDGERVCVDT
     ASMLERGEGM LVGSRSNFMF LVHNESVGSS FTSPRPFRVN AGAVHSYTLG TDGNTLYLSE
     VETGTEVLVL DSHGRARRAA VGRSKIERRP MLMIKAEADG EIGGIIAQDA ETIRFVRPGG
     GLVSVTHLKK GDKVLVHSKP AAGRHFGMEV ADEYILEK