ID   DHQS_METMP              Reviewed;         361 AA.
AC   Q6M1B0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=MMP0006;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   GENE NAME, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=S2 / LL;
RX   PubMed=17010158; DOI=10.1111/j.1365-2958.2006.05426.x;
RA   Porat I., Sieprawska-Lupa M., Teng Q., Bohanon F.J., White R.H.,
RA   Whitman W.B.;
RT   "Biochemical and genetic characterization of an early step in a novel
RT   pathway for the biosynthesis of aromatic amino acids and p-aminobenzoic
RT   acid in the archaeon Methanococcus maripaludis.";
RL   Mol. Microbiol. 62:1117-1131(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   -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not require either
CC       aromatic amino acids (AroAAs) or p-aminobenzoic acid (PABA) for growth,
CC       and growth is similar to that of the wild-type strain in minimal medium
CC       with acetate only. One possible explanation for this unexpected
CC       phenotype is that a second, presently unidentified ORF complements the
CC       function of aroB' in M.maripaludis. {ECO:0000269|PubMed:17010158}.
CC   -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01244}.
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DR   EMBL; BX950229; CAF29562.1; -; Genomic_DNA.
DR   RefSeq; WP_011169950.1; NC_005791.1.
DR   AlphaFoldDB; Q6M1B0; -.
DR   STRING; 267377.MMP0006; -.
DR   DNASU; 2761850; -.
DR   EnsemblBacteria; CAF29562; CAF29562; MMP0006.
DR   GeneID; 2761850; -.
DR   KEGG; mmp:MMP0006; -.
DR   PATRIC; fig|267377.15.peg.6; -.
DR   eggNOG; arCOG04353; Archaea.
DR   HOGENOM; CLU_056379_0_0_2; -.
DR   OMA; HFGMAIK; -.
DR   OrthoDB; 29853at2157; -.
DR   BioCyc; MMAR267377:MMP_RS00060-MON; -.
DR   Proteomes; UP000000590; 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; Reference proteome.
FT   CHAIN           1..361
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_1000067068"
SQ   SEQUENCE   361 AA;  40003 MW;  5F74BBE663AD9B50 CRC64;
     MKFGWIKTTG NDLEERMESV KDALESSIPG IIAEKEEISS VRELGNIKIV SDNLDADVVL
     INKGEDLEIL KSAKLSGKET GVYVVINTKE DEVYATDVSK LDFVDYVVLE GSDWTIIPLE
     NIIADLFSEE IKIVSVVTNV KDAEAAYEIL EKGVDGVVLI PKDINEVKDF SKLIERMNSE
     SVKLDYATVT KIEPVGSGDR VCIDTCSMME MGEGMLIGSY SRGMFLVHSE TVENPYVATR
     PFRVNAGPVH AYILCPENKT KYLSDLKAGD KVLVVNKNGE TREAIIGRVK IEKRPLFLVE
     AEYNGENLRT ILQNAETIRL VGEDGKPVSV VDLKVGTKVL IKPDENARHF GMAIKETIIE
     K