DHQS_NATPD
ID DHQS_NATPD Reviewed; 388 AA.
AC Q3IRN3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=NP_2238A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49210.1; -; Genomic_DNA.
DR RefSeq; WP_011322837.1; NC_007426.1.
DR AlphaFoldDB; Q3IRN3; -.
DR SMR; Q3IRN3; -.
DR STRING; 348780.NP_2238A; -.
DR EnsemblBacteria; CAI49210; CAI49210; NP_2238A.
DR GeneID; 3701388; -.
DR KEGG; nph:NP_2238A; -.
DR eggNOG; arCOG04353; Archaea.
DR HOGENOM; CLU_056379_0_0_2; -.
DR OMA; HFGMAIK; -.
DR OrthoDB; 29853at2157; -.
DR Proteomes; UP000002698; 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..388
FT /note="3-dehydroquinate synthase"
FT /id="PRO_1000067070"
SQ SEQUENCE 388 AA; 42340 MW; E42748E767C31481 CRC64;
MTRSVWLKAD DAVGDWEARK RRITAGLEAG VDWVLVDERD VSRVRELGQV NVAAFAGDDV
HVMDAEEQPD AEPDAVIVGK EGEGDGTVDL PSDFSGSADL TTLRRAEAPA GAYVRILDQD
YESFAETAAV DADYTIVIGD DWQIIPLENL IARIGDETDL IAGVQTAEEA ETAFETLELG
ADAVLLDTDN PDEIRATVEA RDATERETLD LQRATVTEIE ETGSADRVCV DTASMLEHDE
GMLVGSMSRG LFFVHAETAD SPYVASRPFR VNAGAVHAYV RTPDGGTKYL AELSSGDEVQ
VVDTDGNTRE AIVGRAKIEK RPMFRIEAEL ENGDRIETLL QNAETIKVAT DEGRRSVTEL
EAGDELLIYY EDVARHFGEA VEESIIEK
