DHQS_METJA
ID DHQS_METJA Reviewed; 361 AA.
AC Q58646;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=3-dehydroquinate synthase;
DE Short=DHQ synthase;
DE EC=1.4.1.24;
DE AltName: Full=3-dehydroquinate synthase II;
GN Name=aroB'; OrderedLocusNames=MJ1249;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A DHQ SYNTHASE, AND CATALYTIC ACTIVITY.
RX PubMed=15182204; DOI=10.1021/bi0495127;
RA White R.H.;
RT "L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the
RT precursors to the aromatic amino acids in Methanocaldococcus jannaschii.";
RL Biochemistry 43:7618-7627(2004).
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:0000269|PubMed:15182204}.
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;
CC Evidence={ECO:0000269|PubMed:15182204};
CC -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB99252.1; -; Genomic_DNA.
DR PIR; H64455; H64455.
DR RefSeq; WP_010870761.1; NC_000909.1.
DR AlphaFoldDB; Q58646; -.
DR SMR; Q58646; -.
DR STRING; 243232.MJ_1249; -.
DR DNASU; 1452146; -.
DR EnsemblBacteria; AAB99252; AAB99252; MJ_1249.
DR GeneID; 1452146; -.
DR KEGG; mja:MJ_1249; -.
DR eggNOG; arCOG04353; Archaea.
DR HOGENOM; CLU_056379_0_0_2; -.
DR InParanoid; Q58646; -.
DR OMA; HFGMAIK; -.
DR OrthoDB; 29853at2157; -.
DR PhylomeDB; Q58646; -.
DR BioCyc; MetaCyc:MON-14595; -.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
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_0000058769"
SQ SEQUENCE 361 AA; 40260 MW; 8A072D5A4712D7FE CRC64;
MKFGWVNVIG DNWEEKKKIV TTALESSIPV VVAEPEDIEK IKELGNIKVA SHSLDADIVL
VNKNDNIEFL KEAKNLGKET AIYIPIESKE DEEFASEVAR FGFVDNIILE GRDWTIIPLE
NLIADLFHRD VKIVASVNSV DEAKVAYEIL EKGTDGVLLN PKNLEDIKEL SKLIEEMNKE
KVALDVATVT KVEPIGSGDR VCIDTCSLMK IGEGMLIGSY SRALFLVHSE TVENPYVATR
PFRVNAGPVH AYILCPGNKT KYLSELKAGD KVLIVDKDGN TREAIVGRVK IERRPLVLIE
AEYKGDIIRT ILQNAETIRL VNEKGEPISV VDLKPGDKVL IKPEEYARHF GMAIKETIIE
K