AROF_ARATH
ID AROF_ARATH Reviewed; 525 AA.
AC P29976; Q9SMQ7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic;
DE EC=2.5.1.54;
DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 1;
DE AltName: Full=DAHP synthase 1;
DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase 1;
DE Flags: Precursor;
GN Name=DHS1; OrderedLocusNames=At4g39980; ORFNames=T5J17.150;
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 [MRNA].
RX PubMed=1681544; DOI=10.1073/pnas.88.19.8821;
RA Keith B., Dong X.N., Ausubel F.M., Fink G.R.;
RT "Differential induction of 3-deoxy-D-arabino-heptulosonate 7-phosphate
RT synthase genes in Arabidopsis thaliana by wounding and pathogenic attack.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8821-8825(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: By pathogen infection and wounding.
CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC {ECO:0000305}.
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DR EMBL; M74819; AAA32784.1; -; mRNA.
DR EMBL; AL035708; CAB38911.1; -; Genomic_DNA.
DR EMBL; AL161596; CAB80661.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87148.1; -; Genomic_DNA.
DR EMBL; AY090349; AAL91255.1; -; mRNA.
DR EMBL; AY140052; AAM98193.1; -; mRNA.
DR EMBL; BT000821; AAN33196.1; -; mRNA.
DR PIR; A41370; A41370.
DR PIR; T06104; T06104.
DR RefSeq; NP_195708.1; NM_120162.5.
DR AlphaFoldDB; P29976; -.
DR SMR; P29976; -.
DR BioGRID; 15439; 3.
DR IntAct; P29976; 1.
DR STRING; 3702.AT4G39980.1; -.
DR PaxDb; P29976; -.
DR PRIDE; P29976; -.
DR ProteomicsDB; 246966; -.
DR EnsemblPlants; AT4G39980.1; AT4G39980.1; AT4G39980.
DR GeneID; 830159; -.
DR Gramene; AT4G39980.1; AT4G39980.1; AT4G39980.
DR KEGG; ath:AT4G39980; -.
DR Araport; AT4G39980; -.
DR TAIR; locus:2005525; AT4G39980.
DR eggNOG; ENOG502QPP7; Eukaryota.
DR HOGENOM; CLU_026885_0_1_1; -.
DR InParanoid; P29976; -.
DR OMA; QSSFTFH; -.
DR OrthoDB; 546472at2759; -.
DR PhylomeDB; P29976; -.
DR BRENDA; 2.5.1.54; 399.
DR UniPathway; UPA00053; UER00084.
DR PRO; PR:P29976; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P29976; baseline and differential.
DR Genevisible; P29976; AT.
DR GO; GO:0009507; C:chloroplast; TAS:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IDA:TAIR.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; TAS:TAIR.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IDA:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002480; DAHP_synth_2.
DR PANTHER; PTHR21337; PTHR21337; 1.
DR Pfam; PF01474; DAHP_synth_2; 1.
DR TIGRFAMs; TIGR01358; DAHP_synth_II; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..525
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase 1,
FT chloroplastic"
FT /id="PRO_0000002298"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 429..430
FT /note="AP -> ST (in Ref. 1; AAA32784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 57979 MW; 13CA141A3C71D9E6 CRC64;
MALSNASSLS TRSIYGGDLS HRPSNRQSSF TFHPAVNTKP KSVNLVTAVH AAEPARNAVS
VKESVASSSS GALKWTPESW KLKKALQLPD YPNANELESV LKTIEAFPPI VFAGEARNLE
ERLADAAVGK AFLLQGGDCA ESFKEFNATN IRDTFRVLLQ MSIVLTFGGQ VPVIKVGRMA
GQFAKPRSDA FEEKDGVKLP SYKGDNINGD TFDEKSRIPD PNRMIRAYTQ SAATLNLLRA
FATGGYAAIQ RVTQWNLDFV EQSEQADRYQ ELANRVDEAL GFMSACGLGT DHPLMTTTDF
YTSHECLLLP YEQSLTRLDS TSGLYYDCSA HMVWCGERTR QLDGAHVEFL RGIANPLGIK
VSNKMDPFEL VKLVEILNPN NKPGRITVIV RMGAENMRVK LPHLIRAVRR SGQIVTWVCD
PMHGNTIKAP CGLKTRAFDS ILAEVRAFLD VHEQEGSHAG GIHLEMTGQN VTECIGGSRT
VTYDDLSSRY HTHCDPRLNA SQSLELAFIV AERLRKRRTG SQRVS
