ID   DHQS_METS3              Reviewed;         368 AA.
AC   A5UJ82;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Msm_0055;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UJ82; -.
DR   STRING; 420247.Msm_0055; -.
DR   EnsemblBacteria; ABQ86260; ABQ86260; Msm_0055.
DR   KEGG; msi:Msm_0055; -.
DR   PATRIC; fig|420247.28.peg.56; -.
DR   eggNOG; arCOG04353; Archaea.
DR   HOGENOM; CLU_056379_0_0_2; -.
DR   OMA; HFGMAIK; -.
DR   Proteomes; UP000001992; 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..368
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_0000372047"
SQ   SEQUENCE   368 AA;  40380 MW;  2036AC9C9CAC804B CRC64;
     MTPNKPWDDK KEMITTALES GISYVLDLDD YDKIQKLGNV KIVANSDDAD IYLVGINGEG
     DGSLILSEDL NQSQDLQEAK KAKREGKTVC AYVEITDKNH EQLAVSLGSV ADYIILISTD
     WTVIPLENII ADLQKADVKI IAAVADEDGA KLAIETLEHG TDGVIFEAND FNQIKKIAQL
     VVDASKIKYD LKVATVTNVK PLGSGDRVCV DTTDMMKPGE GMLIGSYSKS LFLVHSESLE
     SEYVASRPFR VNAGPVQAYV MVPGNKTRYL SELVAGDEVL IVNTEGETRT AYVGRSKIER
     RPLILIEAEY EGKTIRTLLQ NAETIRIVDA DNNPLSVADI KIGDKVKVYV ESNARHFGIA
     IDETIIEQ