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O22241 (AROD4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arogenate dehydratase 4, chloroplastic

Short name=AtADT4
EC=4.2.1.91
Gene names
Name:ADT4
Ordered Locus Names:At3g44720
ORF Names:T32N15.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Pathway

Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from L-arogenate: step 1/1.

Subcellular location

Plastidchloroplast stroma Ref.6.

Tissue specificity

Expressed in roots, leaves, stems, flowers and siliques. More abundant in stems and roots. Ref.5

Miscellaneous

Has no detectable prehenate dehydratase activity.

Sequence similarities

Contains 1 ACT domain.

Contains 1 prephenate dehydratase domain.

Biophysicochemical properties

Kinetic parameters:

KM=10.08 mM for arogenate Ref.5

Vmax=52.32 pmol/sec/µg enzyme with arogenate as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Chloroplast Potential
Chain35 – 424390Arogenate dehydratase 4, chloroplastic
PRO_0000373793

Regions

Domain126 – 303178Prephenate dehydratase
Domain319 – 41092ACT
Compositional bias244 – 27633Ala-rich

Sequences

Sequence LengthMass (Da)Tools
O22241 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B12A05BE6C0A0D24

FASTA42445,925
        10         20         30         40         50         60 
MQAATSCDLK FRSTDPTSRN KCFSHAIPKR VAVTCGYRSE SFSFPNGVSV SRSDWQSSCA 

        70         80         90        100        110        120 
ILSSKVASVE NTGGLADKIA AVNGHTNGSV NLGLVAVEST NGKLAPAQPL TITDLSPAPL 

       130        140        150        160        170        180 
HGSSLRVAYQ GVPGAYSEAA AGKAYPNCDA IPCDQFDVAF QAVELWIADR AVLPVENSLG 

       190        200        210        220        230        240 
GSIHRNYDLL LRHRLHIVGE VQIPVHHCLL ALPGVRTDCV SRVISHPQAL AQTEHSLDVL 

       250        260        270        280        290        300 
TPHAAREAFH DTAAAAEYIS ANDLHDTAAV ASARAAELYN LQILADGIQD DPGNVTRFLM 

       310        320        330        340        350        360 
LAREPIIPRT DRPFKTSIVF AAQEHKGTSV LFKVLSAFAF RDISLTKIES RPHHNRPLRV 

       370        380        390        400        410        420 
VGDGSFGTSK NFEYMFYVDF EASMAEPRAQ NALAEVQEYT SFLRVLGSYP MDMTPWSMTS 


TEEA 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_190058.1. NM_114340.3.
UniGeneAt.22683.
At.5118.
At.67075.

3D structure databases

ProteinModelPortalO22241.
SMRO22241. Positions 127-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid8921. 10 interactions.
IntActO22241. 13 interactions.
STRING3702.AT3G44720.1-P.

Proteomic databases

PaxDbO22241.
PRIDEO22241.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G44720.1; AT3G44720.1; AT3G44720.
GeneID823601.
KEGGath:AT3G44720.

Organism-specific databases

TAIRAT3G44720.

Phylogenomic databases

eggNOGCOG0077.
HOGENOMHOG000018970.
InParanoidO22241.
KOK05359.
OMAYSHLACK.
PhylomeDBO22241.
ProtClustDBPLN02317.

Enzyme and pathway databases

BioCycARA:AT3G44720-MONOMER.
BRENDA4.2.1.91. 399.
SABIO-RKO22241.
UniPathwayUPA00121; UER00344.

Gene expression databases

GenevestigatorO22241.

Family and domain databases

InterProIPR002912. ACT_dom.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamPF00800. PDT. 1 hit.
[Graphical view]
PROSITEPS51671. ACT. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAROD4_ARATH
AccessionPrimary (citable) accession number: O22241
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names