DHQS_METST
ID DHQS_METST Reviewed; 359 AA.
AC Q2NI00;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Msp_0090;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(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; CP000102; ABC56509.1; -; Genomic_DNA.
DR RefSeq; WP_011405708.1; NC_007681.1.
DR AlphaFoldDB; Q2NI00; -.
DR STRING; 339860.Msp_0090; -.
DR EnsemblBacteria; ABC56509; ABC56509; Msp_0090.
DR GeneID; 41324662; -.
DR KEGG; mst:Msp_0090; -.
DR eggNOG; arCOG04353; Archaea.
DR HOGENOM; CLU_056379_0_0_2; -.
DR OMA; HFGMAIK; -.
DR OrthoDB; 29853at2157; -.
DR Proteomes; UP000001931; 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..359
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000372054"
SQ SEQUENCE 359 AA; 39576 MW; 3DA11A7B2E4A8393 CRC64;
MKFAWIRPNG TWNDRKEAIV DSLESGFDHI MDLDNAETIK KLGSVTIISD KEDSDITLLG
LNNKITMADI KKAQESGKEV AAYVEINNKD DELLVSKLGT VADYVILKGK NWKVIPLENI
IASLQNRTSK IIVDVPNYEE AKLALETMEH GSDGVLLSSN DGNEIRKLGA LIEKVSKESY
DLKAATVTKV ESVGIGDRVC VDTCSMMNVG DGMLVGSFAS GLFLVHSETL ESEYVASRPF
RVNAGPVHAY VMTPENKTRY LSELEAGDEV VTLNSKGEAN TVIVGRVKIE KRPLLLIEAK
YKNSRIRTLV QNAETIRLVN DKGEPISVSK LKVGDKVLAY FSEAARHFGM AIEEQIIEK
