AROD2_ARATH
ID AROD2_ARATH Reviewed; 381 AA.
AC Q9SSE7; Q8LFI1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Arogenate dehydratase/prephenate dehydratase 2, chloroplastic {ECO:0000303|PubMed:17726025, ECO:0000303|Ref.1};
DE Short=AtADT2 {ECO:0000303|PubMed:17726025, ECO:0000303|Ref.1};
DE Short=AtPDT2 {ECO:0000303|PubMed:17726025};
DE EC=4.2.1.51 {ECO:0000269|PubMed:17726025};
DE EC=4.2.1.91 {ECO:0000269|PubMed:17726025};
DE Flags: Precursor;
GN Name=ADT2 {ECO:0000303|PubMed:17726025, ECO:0000303|Ref.1};
GN Synonyms=PDT2 {ECO:0000303|PubMed:17726025};
GN OrderedLocusNames=At3g07630 {ECO:0000312|Araport:AT3G07630};
GN ORFNames=MLP3.8 {ECO:0000312|EMBL:AAF13081.1};
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].
RC STRAIN=cv. Columbia;
RA Matringe M., Grisollet D., Rippert P.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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).
RN [5]
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RX PubMed=17726025; DOI=10.1074/jbc.m702662200;
RA Cho M.-H., Corea O.R.A., Yang H., Bedgar D.L., Laskar D.D., Anterola A.M.,
RA Moog-Anterola F.A., Hood R.L., Kohalmi S.E., Bernards M.A., Kang C.,
RA Davin L.B., Lewis N.G.;
RT "Phenylalanine biosynthesis in Arabidopsis thaliana. Identification and
RT characterization of arogenate dehydratases.";
RL J. Biol. Chem. 282:30827-30835(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19136569; DOI=10.1104/pp.108.130070;
RA Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M.;
RT "Tyrosine and phenylalanine are synthesized within the plastids in
RT Arabidopsis.";
RL Plant Physiol. 149:1251-1260(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=30252596; DOI=10.1080/15592324.2018.1517075;
RA Abolhassani Rad S., Clayton E.J., Cornelius E.J., Howes T.R., Kohalmi S.E.;
RT "Moonlighting proteins: putting the spotlight on enzymes.";
RL Plant Signal. Behav. 13:e1517075-e1517075(2018).
CC -!- FUNCTION: Converts the prephenate produced from the shikimate-
CC chorismate pathway into phenylalanine (PubMed:17726025). Dehydratase
CC that uses arogenate and prephenate as substrates (PubMed:17726025).
CC Utilzes more efficiently arogenate than prephenate (PubMed:17726025).
CC Required for chloroplast division prior to ARC5, but in an ARC3- and
CC ARC6-dependent manner, especially involved in the Z-ring formation
CC (PubMed:30252596). {ECO:0000269|PubMed:17726025,
CC ECO:0000269|PubMed:30252596}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arogenate = CO2 + H2O + L-phenylalanine;
CC Xref=Rhea:RHEA:12536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58095, ChEBI:CHEBI:58180; EC=4.2.1.91;
CC Evidence={ECO:0000269|PubMed:17726025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12537;
CC Evidence={ECO:0000269|PubMed:17726025};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC Evidence={ECO:0000269|PubMed:17726025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21649;
CC Evidence={ECO:0000269|PubMed:17726025};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.80 mM for arogenate {ECO:0000269|PubMed:17726025};
CC KM=0.68 mM for prephenate {ECO:0000269|PubMed:17726025};
CC Vmax=60.60 pmol/sec/ug enzyme with arogenate as substrate
CC {ECO:0000269|PubMed:17726025};
CC Vmax=1.6 pmol/sec/ug enzyme with prephenate as substrate
CC {ECO:0000269|PubMed:17726025};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC phenylalanine from L-arogenate: step 1/1.
CC {ECO:0000269|PubMed:17726025}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000269|PubMed:17726025}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19136569, ECO:0000269|PubMed:30252596}.
CC Note=Observed in chloroplast stromules, and as a ring around the
CC equatorial plane of dividing plastids, thus colocalizing with FtsZ1 and
CC FtsZ2. {ECO:0000269|PubMed:30252596}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. Most abundant in leaves and seeds.
CC {ECO:0000269|PubMed:17726025}.
CC -!- DISRUPTION PHENOTYPE: Large and misshapen chloroplasts with distorted
CC and irregular outlines. {ECO:0000269|PubMed:30252596}.
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DR EMBL; DQ411465; ABD67751.1; -; mRNA.
DR EMBL; AC009176; AAF13081.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74577.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74578.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63416.1; -; Genomic_DNA.
DR EMBL; AY050813; AAK92748.1; -; mRNA.
DR EMBL; AY113967; AAM45015.1; -; mRNA.
DR EMBL; AY084830; AAM61395.1; -; mRNA.
DR RefSeq; NP_001325505.1; NM_001337726.1.
DR RefSeq; NP_187420.1; NM_111642.3.
DR RefSeq; NP_974249.1; NM_202520.2.
DR AlphaFoldDB; Q9SSE7; -.
DR SMR; Q9SSE7; -.
DR STRING; 3702.AT3G07630.1; -.
DR PaxDb; Q9SSE7; -.
DR PRIDE; Q9SSE7; -.
DR ProteomicsDB; 246958; -.
DR EnsemblPlants; AT3G07630.1; AT3G07630.1; AT3G07630.
DR EnsemblPlants; AT3G07630.2; AT3G07630.2; AT3G07630.
DR EnsemblPlants; AT3G07630.3; AT3G07630.3; AT3G07630.
DR GeneID; 819954; -.
DR Gramene; AT3G07630.1; AT3G07630.1; AT3G07630.
DR Gramene; AT3G07630.2; AT3G07630.2; AT3G07630.
DR Gramene; AT3G07630.3; AT3G07630.3; AT3G07630.
DR KEGG; ath:AT3G07630; -.
DR Araport; AT3G07630; -.
DR TAIR; locus:2091127; AT3G07630.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_035008_4_0_1; -.
DR InParanoid; Q9SSE7; -.
DR OMA; PLMIYRE; -.
DR OrthoDB; 1090069at2759; -.
DR PhylomeDB; Q9SSE7; -.
DR BioCyc; ARA:AT3G07630-MON; -.
DR BRENDA; 4.2.1.91; 399.
DR SABIO-RK; Q9SSE7; -.
DR UniPathway; UPA00121; UER00344.
DR UniPathway; UPA00121; UER00345.
DR PRO; PR:Q9SSE7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SSE7; baseline and differential.
DR Genevisible; Q9SSE7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010319; C:stromule; IDA:UniProtKB.
DR GO; GO:0047769; F:arogenate dehydratase activity; IDA:TAIR.
DR GO; GO:0004664; F:prephenate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR Pfam; PF00800; PDT; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Lyase; Phenylalanine biosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..381
FT /note="Arogenate dehydratase/prephenate dehydratase 2,
FT chloroplastic"
FT /id="PRO_0000373791"
FT DOMAIN 100..275
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 289..375
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 25
FT /note="P -> S (in Ref. 5; AAM61395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42115 MW; 04AC7EB3988B0AF7 CRC64;
MAMHTVRLSP ATQLHGGISS NLSPPNRKPN NSIVRYGCGS SKRFRIVTVL ASLRENDANG
RDNSVRAMEV KKIFEDSPLL PKPLSSNQLT ESVSNGSRVR VAYQGVRGAY SESAAEKAYP
NCEAVPCEEF DTAFEAVERW LVDRAVLPIE NSLGGSIHRN YDLLLRHNLH IVGEVKLAVR
HCLLANHGVN IEDLRRVLSH PQALAQCENT LTKLGLVREA VDDTAGAAKQ IAFENLNDAA
AVASEKAAKI YGLNIVAKDI QDDCDNVTRF LMLAREPIIP GTNRLFKTSI VFSLEEGPGV
LFKALAVFAL RQINLTKIES RPLRKHPLRA SGGLKYFDYL FYVDFEASMA DEVAQNALRH
LEEFATFLRV LGSYPVDTTM L
