Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Arogenate dehydratase 4, chloroplastic

Gene

ADT4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine.1 Publication

Catalytic activityi

L-arogenate = L-phenylalanine + H2O + CO2.

Kineticsi

  1. KM=10.08 mM for arogenate1 Publication
  1. Vmax=52.32 pmol/sec/µg enzyme with arogenate as substrate1 Publication

Pathway: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-phenylalanine from L-arogenate.
Proteins known to be involved in this subpathway in this organism are:
  1. Arogenate dehydratase/prephenate dehydratase 1, chloroplastic (ADT1), Arogenate dehydratase 5, chloroplastic (ADT5), Arogenate dehydratase 4, chloroplastic (ADT4), Arogenate dehydratase 3, chloroplastic (ADT3), Arogenate dehydratase/prephenate dehydratase 2, chloroplastic (ADT2), Arogenate dehydratase/prephenate dehydratase 6, chloroplastic (ADT6)
This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-phenylalanine from L-arogenate, the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • L-phenylalanine biosynthetic process Source: UniProtKB-UniPathway
  • response to karrikin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

Enzyme and pathway databases

BioCyciARA:AT3G44720-MONOMER.
BRENDAi4.2.1.91. 399.
SABIO-RKO22241.
UniPathwayiUPA00121; UER00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Arogenate dehydratase 4, chloroplastic (EC:4.2.1.91)
Short name:
AtADT4
Gene namesi
Name:ADT4
Ordered Locus Names:At3g44720
ORF Names:T32N15.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G44720.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434ChloroplastSequence AnalysisAdd
BLAST
Chaini35 – 424390Arogenate dehydratase 4, chloroplasticPRO_0000373793Add
BLAST

Proteomic databases

PaxDbiO22241.
PRIDEiO22241.

Expressioni

Tissue specificityi

Expressed in roots, leaves, stems, flowers and siliques. More abundant in stems and roots.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi8921. 10 interactions.
IntActiO22241. 13 interactions.
STRINGi3702.AT3G44720.1.

Structurei

3D structure databases

ProteinModelPortaliO22241.
SMRiO22241. Positions 127-409.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 303178Prephenate dehydratasePROSITE-ProRule annotationAdd
BLAST
Domaini319 – 41092ACTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi244 – 27633Ala-richAdd
BLAST

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation
Contains 1 prephenate dehydratase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0077.
HOGENOMiHOG000018970.
InParanoidiO22241.
KOiK05359.
OMAiYSHLACK.
PhylomeDBiO22241.

Family and domain databases

InterProiIPR002912. ACT_dom.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF00800. PDT. 1 hit.
[Graphical view]
PROSITEiPS51671. ACT. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O22241-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAATSCDLK FRSTDPTSRN KCFSHAIPKR VAVTCGYRSE SFSFPNGVSV
60 70 80 90 100
SRSDWQSSCA ILSSKVASVE NTGGLADKIA AVNGHTNGSV NLGLVAVEST
110 120 130 140 150
NGKLAPAQPL TITDLSPAPL HGSSLRVAYQ GVPGAYSEAA AGKAYPNCDA
160 170 180 190 200
IPCDQFDVAF QAVELWIADR AVLPVENSLG GSIHRNYDLL LRHRLHIVGE
210 220 230 240 250
VQIPVHHCLL ALPGVRTDCV SRVISHPQAL AQTEHSLDVL TPHAAREAFH
260 270 280 290 300
DTAAAAEYIS ANDLHDTAAV ASARAAELYN LQILADGIQD DPGNVTRFLM
310 320 330 340 350
LAREPIIPRT DRPFKTSIVF AAQEHKGTSV LFKVLSAFAF RDISLTKIES
360 370 380 390 400
RPHHNRPLRV VGDGSFGTSK NFEYMFYVDF EASMAEPRAQ NALAEVQEYT
410 420
SFLRVLGSYP MDMTPWSMTS TEEA
Length:424
Mass (Da):45,925
Last modified:January 1, 1998 - v1
Checksum:iB12A05BE6C0A0D24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ411467 mRNA. Translation: ABD67753.1.
AC002534 Genomic DNA. Translation: AAB70035.1.
CP002686 Genomic DNA. Translation: AEE77939.1.
AY062692 mRNA. Translation: AAL32770.1.
BT008862 mRNA. Translation: AAP68301.1.
RefSeqiNP_190058.1. NM_114340.3.
UniGeneiAt.22683.
At.5118.
At.67075.

Genome annotation databases

EnsemblPlantsiAT3G44720.1; AT3G44720.1; AT3G44720.
GeneIDi823601.
KEGGiath:AT3G44720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ411467 mRNA. Translation: ABD67753.1.
AC002534 Genomic DNA. Translation: AAB70035.1.
CP002686 Genomic DNA. Translation: AEE77939.1.
AY062692 mRNA. Translation: AAL32770.1.
BT008862 mRNA. Translation: AAP68301.1.
RefSeqiNP_190058.1. NM_114340.3.
UniGeneiAt.22683.
At.5118.
At.67075.

3D structure databases

ProteinModelPortaliO22241.
SMRiO22241. Positions 127-409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi8921. 10 interactions.
IntActiO22241. 13 interactions.
STRINGi3702.AT3G44720.1.

Proteomic databases

PaxDbiO22241.
PRIDEiO22241.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G44720.1; AT3G44720.1; AT3G44720.
GeneIDi823601.
KEGGiath:AT3G44720.

Organism-specific databases

TAIRiAT3G44720.

Phylogenomic databases

eggNOGiCOG0077.
HOGENOMiHOG000018970.
InParanoidiO22241.
KOiK05359.
OMAiYSHLACK.
PhylomeDBiO22241.

Enzyme and pathway databases

UniPathwayiUPA00121; UER00344.
BioCyciARA:AT3G44720-MONOMER.
BRENDAi4.2.1.91. 399.
SABIO-RKO22241.

Miscellaneous databases

PROiO22241.

Family and domain databases

InterProiIPR002912. ACT_dom.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF00800. PDT. 1 hit.
[Graphical view]
PROSITEiPS51671. ACT. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiAROD4_ARATH
AccessioniPrimary (citable) accession number: O22241
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Has no detectable prehenate dehydratase activity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.