ID V5TQ62_HALHI Unreviewed; 388 AA.
AC V5TQ62;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_01244};
DE Short=DHQ synthase {ECO:0000256|HAMAP-Rule:MF_01244};
DE EC=1.4.1.24 {ECO:0000256|HAMAP-Rule:MF_01244};
DE AltName: Full=3-dehydroquinate synthase II {ECO:0000256|HAMAP-Rule:MF_01244};
GN Name=aroB' {ECO:0000256|HAMAP-Rule:MF_01244};
GN ORFNames=HISP_12195 {ECO:0000313|EMBL:AHB66729.1};
OS Haloarcula hispanica N601.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=1417673 {ECO:0000313|Proteomes:UP000018572};
RN [1] {ECO:0000313|EMBL:AHB66729.1, ECO:0000313|Proteomes:UP000018572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N601 {ECO:0000313|EMBL:AHB66729.1,
RC ECO:0000313|Proteomes:UP000018572};
RX PubMed=24625874;
RA Ding J.Y., Chiang P.W., Hong M.J., Dyall-Smith M., Tang S.L.;
RT "Complete Genome Sequence of the Extremely Halophilic Archaeon Haloarcula
RT hispanica Strain N601.";
RL Genome Announc. 2:e00178-14(2014).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01244};
CC -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_01244}.
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; CP006884; AHB66729.1; -; Genomic_DNA.
DR RefSeq; WP_014041086.1; NC_023013.1.
DR AlphaFoldDB; V5TQ62; -.
DR GeneID; 25154998; -.
DR KEGG; hhn:HISP_12195; -.
DR HOGENOM; CLU_056379_0_0_2; -.
DR Proteomes; UP000018572; Chromosome 1.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01244; Arch_DHQ_synthase; 1.
DR InterPro; IPR002812; DHQ_synth.
DR PANTHER; PTHR33563; -; 1.
DR PANTHER; PTHR33563:SF1; 3-DEHYDROQUINATE SYNTHASE; 1.
DR Pfam; PF01959; DHQS; 1.
DR PIRSF; PIRSF006655; DHQ_synth; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01244};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_01244}; NAD {ECO:0000256|HAMAP-Rule:MF_01244};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01244}.
SQ SEQUENCE 388 AA; 42370 MW; 782D441FF902B890 CRC64;
MTRSVWLKAD SEVGDWETRK RRITAGIEAG VDWVLVDEED VDRASELGEI NIAAFTNGDV
HVMEAEAEDS GADATIVGKD GEGDGTVDLP SDFSGSADLS TLRQNGAAPD GGYVRIFDED
YEAFAEAVAA EADFTIVIGE NWQIIPLENL IARVGEETDL IAGVRTAEDA RTAYETLEIG
ADGVLLDTDD LDEIRKTVEV RDEMGRESLD LEYAEVTAIE QTGSADRVCI DTGSLMEHDE
GMLVGSMARG LFFVHAETAE SPYVASRPFR VNAGAVHAYV RTPDGGTKYL SELQSGDEVQ
IVDADGHTRE AIVGRAKIEK RPMFRVQAET EDGDRIETLL QNAETIKVHT RDGRTAVTNL
EPGDEILIYH EDTATHFGER IEESIIEK
//
