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DHQS_METBF
ID   DHQS_METBF              Reviewed;         380 AA.
AC   Q46DZ8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Mbar_A0921;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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; CP000099; AAZ69894.1; -; Genomic_DNA.
DR   RefSeq; WP_011305943.1; NC_007355.1.
DR   AlphaFoldDB; Q46DZ8; -.
DR   STRING; 269797.Mbar_A0921; -.
DR   EnsemblBacteria; AAZ69894; AAZ69894; Mbar_A0921.
DR   GeneID; 3627301; -.
DR   KEGG; mba:Mbar_A0921; -.
DR   eggNOG; arCOG04353; Archaea.
DR   HOGENOM; CLU_056379_0_0_2; -.
DR   OMA; HFGMAIK; -.
DR   OrthoDB; 29853at2157; -.
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..380
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_1000067065"
SQ   SEQUENCE   380 AA;  41504 MW;  F7DDBD1E8E88A3D8 CRC64;
     MKKKSVWIKA DEGGWEQQKE RITTGLESGA DCVLVNPGDV GKVRELGNIP VATFGRDNKS
     GAEIIVVGKR GEGDGTKPLP LETQGSLDIN AATLLRDKEV AVGGYVIIKD KRYEQFAAEM
     GKVCDFLIVT GTDWKVIPLE NLIAELQRYD VKIIFGVKNA EEARLAFKTL ETGADGVLLN
     SGNIQEIKDT IQAAREMENE RTELESAVIT RVEPLGMGDR VCVDTCNLMQ KGEGMLIGSQ
     ASGMFLVNSE SDDSPYVAAR PFRVNAGAVH SYIKIGDKTR YLSELRTGDA VTIIDSKGRQ
     REGFVGRVKI ESRPLMLIEA KAGNRTLSAI LQNAETIKLV GKDGNPISVA KLKKGDEVLV
     RLEEGARHFG KKIEETIIEK
 
 
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