DHQS_SOLLC
ID DHQS_SOLLC Reviewed; 442 AA.
AC Q8RU74;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=3-dehydroquinate synthase, chloroplastic;
DE EC=4.2.3.4;
DE Flags: Precursor;
GN Name=DHQS; Synonyms=AROB; OrderedLocusNames=Solyc02g083590;
GN ORFNames=LOC544273;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY ELICITOR.
RC STRAIN=cv. UC82B;
RX PubMed=8704160; DOI=10.1007/bf00020607;
RA Bischoff M., Rosler J., Raesecke H.R., Gorlach J., Amrhein N., Schmid J.;
RT "Cloning of a cDNA encoding a 3-dehydroquinate synthase from a higher
RT plant, and analysis of the organ-specific and elicitor-induced expression
RT of the corresponding gene.";
RL Plant Mol. Biol. 31:69-76(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Catalyzes the second step in the shikimate pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Lower expression in
CC stems, flowers and cotyledons. Barely detected in leaves.
CC {ECO:0000269|PubMed:8704160}.
CC -!- INDUCTION: Up-regulated by elicitor. {ECO:0000269|PubMed:8704160}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000305}.
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DR EMBL; L46847; AAL77575.1; -; mRNA.
DR RefSeq; NP_001233863.1; NM_001246934.1.
DR AlphaFoldDB; Q8RU74; -.
DR SMR; Q8RU74; -.
DR STRING; 4081.Solyc02g083590.2.1; -.
DR PaxDb; Q8RU74; -.
DR PRIDE; Q8RU74; -.
DR GeneID; 544273; -.
DR KEGG; sly:544273; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_001201_0_2_1; -.
DR InParanoid; Q8RU74; -.
DR OrthoDB; 558864at2759; -.
DR PhylomeDB; Q8RU74; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000004994; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; TAS:UniProtKB.
DR HAMAP; MF_00110; DHQ_synthase; 1.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030960; DHQS/DOIS.
DR Pfam; PF01761; DHQ_synthase; 1.
DR TIGRFAMs; TIGR01357; aroB; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Lyase; Metal-binding; NAD; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..442
FT /note="3-dehydroquinate synthase, chloroplastic"
FT /id="PRO_0000425859"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 183..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 208..209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 248..251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 442 AA; 48123 MW; 526ECFB73ED87C8A CRC64;
MASSFCPKQA LSFTNSTHQL HQSRAIPRDI HVRFPAPVSS PSSRCGLKSK ATTRLKVLAT
SATKVMDHSS SKASSQAPTV VEVDLGTRSY PIYIGAGLLD QPDLLQRHIH GKRVLVVTNT
TVAPLYLDKT ISALTDGNPN VTVESVILPD GEQFKNMETL MKVFDKAIES RLDRRCTFVA
LGGGVIGDMC GYAAASYLRG VNFIQIPTTV MAQVDSSVGG KTGINHPLGK NMIGAFYQPQ
CVLIDTDTLN TLPDRELASG LAEVIKYGLI RDAEFFEWQE QNMPLLLARD PTAFTYAIKR
SCENKADVVS QDEKESGVRA TLNLGHTFGH AVETGVGYGQ WLHGEAVAAG TVMAVDMSRR
LGWIDDSLVQ RVQKILQQAK LPTSPPETMT VEMFKSIMAV DKKVADGKLR LILLKGSLGN
CVFTGDYDQK ALDETLRAFS KS
