DHQS_ARATH
ID DHQS_ARATH Reviewed; 442 AA.
AC Q8VYV7; F4JZ33; Q8LFK9; Q9FKX0;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=3-dehydroquinate synthase, chloroplastic;
DE EC=4.2.3.4;
DE Flags: Precursor;
GN Name=DHQS; Synonyms=AROB; OrderedLocusNames=At5g66120; ORFNames=K2A18.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-59, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ARG-58, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the second step in the shikimate pathway.
CC {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VYV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VYV7-2; Sequence=VSP_053869;
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10417.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB011474; BAB10417.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED98161.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98162.1; -; Genomic_DNA.
DR EMBL; AY069891; AAL47443.1; -; mRNA.
DR EMBL; AY142020; AAM98284.1; -; mRNA.
DR EMBL; AY084788; AAM61355.1; -; mRNA.
DR RefSeq; NP_569029.1; NM_126010.3. [Q8VYV7-1]
DR RefSeq; NP_851279.1; NM_180948.2. [Q8VYV7-2]
DR AlphaFoldDB; Q8VYV7; -.
DR SMR; Q8VYV7; -.
DR BioGRID; 21986; 3.
DR STRING; 3702.AT5G66120.2; -.
DR iPTMnet; Q8VYV7; -.
DR PaxDb; Q8VYV7; -.
DR PRIDE; Q8VYV7; -.
DR ProteomicsDB; 224056; -. [Q8VYV7-1]
DR EnsemblPlants; AT5G66120.1; AT5G66120.1; AT5G66120. [Q8VYV7-2]
DR EnsemblPlants; AT5G66120.2; AT5G66120.2; AT5G66120. [Q8VYV7-1]
DR GeneID; 836744; -.
DR Gramene; AT5G66120.1; AT5G66120.1; AT5G66120. [Q8VYV7-2]
DR Gramene; AT5G66120.2; AT5G66120.2; AT5G66120. [Q8VYV7-1]
DR KEGG; ath:AT5G66120; -.
DR Araport; AT5G66120; -.
DR TAIR; locus:2156942; AT5G66120.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_001201_0_2_1; -.
DR InParanoid; Q8VYV7; -.
DR OMA; IKMAVCF; -.
DR PhylomeDB; Q8VYV7; -.
DR BioCyc; ARA:AT5G66120-MON; -.
DR UniPathway; UPA00053; UER00085.
DR PRO; PR:Q8VYV7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VYV7; baseline and differential.
DR Genevisible; Q8VYV7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
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; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Chloroplast; Lyase; Metal-binding; NAD;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 59..442
FT /note="3-dehydroquinate synthase, chloroplastic"
FT /id="PRO_0000425860"
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"
FT MOD_RES 59
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..106
FT /note="MAANTISLSNVAASKNLNSFQSRAFIAPPTIFFPVASAKSKPGELSLSSTTL
FT SRSRVRAGASQLMNEPLNDQRSISSPTVVEVDLGDRSYPIYIGAGLLDHSELLQ -> M
FT F (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053869"
FT CONFLICT 260
FT /note="G -> D (in Ref. 4; AAM61355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 48064 MW; D592DFC755DDDC7A CRC64;
MAANTISLSN VAASKNLNSF QSRAFIAPPT IFFPVASAKS KPGELSLSST TLSRSRVRAG
ASQLMNEPLN DQRSISSPTV VEVDLGDRSY PIYIGAGLLD HSELLQRHVH GKRVLVVTND
RVAPLYLDKT IDALTRGNPN VTVESVILPD GEKYKDMDTL MKVFDKAIES RLDRRCTFVA
LGGGVIGDMC GYAAASYLRG VNFIQIPTTV MAQVDSSVGG KTGINHRLGK NLIGAFYQPQ
CVLVDTDTLN TLPDREMASG LAEVIKYGLI RDAEFFEWQE KNIEALLARD PAALAFAIKR
SCENKADVVS QDEKESGLRA TLNLGHTFGH AIETGFGYGE WLHGEAVAAG TVMAVDMSYR
LGWIDESIVK RVNKILVRAK LPTTPPESMT VSMFKSIMAV DKKVADGLLR LILLKGPLGN
CVFTGDYDRE ALDATLRAFS KS
