Reviewed, UniProtKB/Swiss-Prot Q9SSE7 (AROD2_ARATH)

Names and origin

Protein names

Recommended name:
    Arogenate dehydratase/prephenate dehydratase 2, chloroplastic
      Short name=AtADT2
      Short name=AtPDT2
    EC=4.2.1.91
    EC=4.2.1.51

Gene names

Name:	ADT2
Synonyms:	PDT2
Ordered Locus Names:	At3g07630
ORF Names:	MLP3.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine. Ref.5
Catalytic activity	L-arogenate = L-phenylalanine + H2O + CO2. Prephenate = phenylpyruvate + H2O + CO2.
Pathway	Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from L-arogenate: step 1/1. Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Subcellular location	Plastid › chloroplast stroma. Ref.6
Tissue specificity	Expressed in roots, leaves, stems, flowers and siliques. Most abundant in leaves and seeds. Ref.5
Sequence similarities	Contains 1 ACT domain. Contains 1 prephenate dehydratase domain.
Biophysicochemical properties	Kinetic parameters: KM=0.80 mM for arogenate KM=0.68 mM for prephenate Vmax=60.60 pmol/sec/µg enzyme with arogenate as substrate Vmax=1.6 pmol/sec/µg enzyme with prephenate as substrate

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Phenylalanine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-phenylalanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	amino acid binding Inferred from electronic annotation. Source: InterPro arogenate dehydratase activity Ref.5 Inferred from direct assay. Source: TAIR prephenate dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 66	66	Chloroplast Potential
	Chain	67 – 381	315	Arogenate dehydratase/prephenate dehydratase 2, chloroplastic		PRO_0000373791
Regions
	Domain	100 – 275	176	Prephenate dehydratase
	Domain	288 – 366	79	ACT
Experimental info
	Sequence conflict	25	1	P → S in AAM61395. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9SSE7-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 04AC7EB3988B0AF7	FASTA	381	42,115
	10 20 30 40 50 60 MAMHTVRLSP ATQLHGGISS NLSPPNRKPN NSIVRYGCGS SKRFRIVTVL ASLRENDANG 70 80 90 100 110 120 RDNSVRAMEV KKIFEDSPLL PKPLSSNQLT ESVSNGSRVR VAYQGVRGAY SESAAEKAYP 130 140 150 160 170 180 NCEAVPCEEF DTAFEAVERW LVDRAVLPIE NSLGGSIHRN YDLLLRHNLH IVGEVKLAVR 190 200 210 220 230 240 HCLLANHGVN IEDLRRVLSH PQALAQCENT LTKLGLVREA VDDTAGAAKQ IAFENLNDAA 250 260 270 280 290 300 AVASEKAAKI YGLNIVAKDI QDDCDNVTRF LMLAREPIIP GTNRLFKTSI VFSLEEGPGV 310 320 330 340 350 360 LFKALAVFAL RQINLTKIES RPLRKHPLRA SGGLKYFDYL FYVDFEASMA DEVAQNALRH 370 380 LEEFATFLRV LGSYPVDTTM L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Matringe M., Grisollet D., Rippert P. Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Phenylalanine biosynthesis in Arabidopsis thaliana. Identification and characterization of arogenate dehydratases." Cho M.-H., Corea O.R.A., Yang H., Bedgar D.L., Laskar D.D., Anterola A.M., Moog-Anterola F.A., Hood R.L., Kohalmi S.E., Bernards M.A., Kang C., Davin L.B., Lewis N.G. J. Biol. Chem. 282:30827-30835(2007) [PubMed: 17726025] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[6]	"Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis." Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M. Plant Physiol. 149:1251-1260(2009) [PubMed: 19136569] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ411465 mRNA. Translation: ABD67751.1. AC009176 Genomic DNA. Translation: AAF13081.1. AY050813 mRNA. Translation: AAK92748.1. AY113967 mRNA. Translation: AAM45015.1. AY084830 mRNA. Translation: AAM61395.1.
IPI	IPI00528286.
RefSeq	NP_187420.1. NP_974249.1.
UniGene	At.22712
3D structure databases
HSSP	HSSP built from PDB template 1PHZ based on UniProtKB P04176.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SSE7.
Proteomic databases
PRIDE	Q9SSE7.
Genome annotation databases
GeneID	819954.
GenomeReviews	Gene locus AT3G07630 in contig BA000014_GR.
KEGG	ath:AT3G07630.
NMPDR	fig|3702.1.peg.12794.
Organism-specific databases
TAIR	At3g07630.
Phylogenomic databases
OMA	YSESAAE.
Gene expression databases
ArrayExpress	Q9SSE7.
Genevestigator	Q9SSE7.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001086. Preph_deHydtase. IPR018528. Preph_deHydtase_CS. [Graphical view]
Pfam	PF01842. ACT. 1 hit. PF00800. PDT. 1 hit. [Graphical view]
PROSITE	PS00857. PREPHENATE_DEHYDR_1. 1 hit. PS00858. PREPHENATE_DEHYDR_2. 1 hit. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AROD2_ARATH

Accession

Primary (citable) accession number: Q9SSE7
Secondary accession number(s): Q8LFI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)