DHQS_HALWD
ID DHQS_HALWD Reviewed; 399 AA.
AC Q18DY6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=HQ_1155A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(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; AM180088; CAJ51285.1; -; Genomic_DNA.
DR RefSeq; WP_011570450.1; NC_008212.1.
DR AlphaFoldDB; Q18DY6; -.
DR STRING; 362976.HQ_1155A; -.
DR EnsemblBacteria; CAJ51285; CAJ51285; HQ_1155A.
DR GeneID; 4193719; -.
DR KEGG; hwa:HQ_1155A; -.
DR eggNOG; arCOG04353; Archaea.
DR HOGENOM; CLU_056379_0_0_2; -.
DR OMA; HFGMAIK; -.
DR Proteomes; UP000001975; 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..399
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000372045"
SQ SEQUENCE 399 AA; 43552 MW; 18870C9295C4E970 CRC64;
MTESRSHSRR VWIKADSDVG DWKTRKRRIT TGLEAGVDCV LVDPEDISRV QSLGDVSIAA
FTSTADSETD SSAETEGVEE ADTVVIGKES ESDGTDDFPE TLSASADLSA IETHSNNTVV
ETGAYIRILS EEYEALAETA AADASYTIVI GEDWTIIPLE NLIARIGSET TLIAGVTSAE
EAQTAFETLE IGADGVLLDT DDPDEIRETV AVRDATERET LELEWATVID IERAGMADRV
CVDTANLMQH NEGMLIGSMS RGLIFVHAET AESPYIASRP FRVNAGAVHA YLRTPDGGTA
YLSELQSGDT VQVVNTDGQT REAIVGRVKI EKRPMFRIEL EYDDDRVETL LQNAETIKVN
TQSGRTAVTD LESGDEIRLF YEETARHFGE AVEESIIEK