ID   DHQS_METAC              Reviewed;         380 AA.
AC   Q8THC5;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=MA_4592;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM07931.1; -; Genomic_DNA.
DR   RefSeq; WP_011024465.1; NC_003552.1.
DR   AlphaFoldDB; Q8THC5; -.
DR   STRING; 188937.MA_4592; -.
DR   EnsemblBacteria; AAM07931; AAM07931; MA_4592.
DR   GeneID; 1476486; -.
DR   KEGG; mac:MA_4592; -.
DR   HOGENOM; CLU_056379_0_0_2; -.
DR   InParanoid; Q8THC5; -.
DR   OMA; HFGMAIK; -.
DR   OrthoDB; 29853at2157; -.
DR   PhylomeDB; Q8THC5; -.
DR   Proteomes; UP000002487; 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   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01244; Arch_DHQ_synthase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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..380
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_0000058768"
SQ   SEQUENCE   380 AA;  41353 MW;  3026FFCE4649C82B CRC64;
     MKKKSVWIKA DEGGWEEQKD RITTGLESGA DCVLVNPGDV EKVRELGNIT VAAFARDNKS
     RADIVVVGKR GEGDGTKPLP QEIPGSFDIN AATLLMDKGV TVGGYVVIKD KHYEHFAAEM
     GKICDYLLVT GTDWKVIPLE NLIADLQHQK VKIIFGVKSA EEARLAFQTL EAGADGVLLD
     SGNPQEIKDT IKAARELESE SAELEAAVVT RVEPLGMGDR VCVDTCNLMQ RGEGMLIGSQ
     ASGMFLVNSE SDDSPYVAAR PFRVNAGAVH SYIKIGEKTR YLSELRAGDP VTIVDSKGKQ
     REGIVGRVKI ESRPLMLIEA KARDRTLTAI LQNAETIKLV GKDGTPISVA KLEKGDEVLV
     RLEEGARHFG KKIEETIIEK