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Q9LR29 (TAR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. 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:
Tryptophan aminotransferase-related protein 1

EC=2.6.1.27
EC=2.6.1.99
Gene names
Name:TAR1
Ordered Locus Names:At1g23320
ORF Names:F26F24.17
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probably involved in auxin production. TAA1, TAR1 and TAR2 are required for proper embryo patterning. Ref.3

Catalytic activity

L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate.

L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Enzyme regulation

Inhibited by L-kynurenine. Ref.5

Pathway

Plant hormone metabolism; auxin biosynthesis.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Very low expression in seedlings. Ref.3

Induction

Slightly up-regulated by ethylene. Ref.3 Ref.5

Disruption phenotype

No visible phenotype. Ref.3

Sequence similarities

Belongs to the alliinase family.

Sequence caution

The sequence AAF87014.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Tryptophan aminotransferase-related protein 1
PRO_0000411674

Regions

Region101 – 1022Pyridoxal phosphate binding By similarity
Region190 – 1934Pyridoxal phosphate binding By similarity
Region213 – 2164Pyridoxal phosphate binding By similarity

Sites

Binding site591Pyridoxal phosphate By similarity
Binding site1691Pyridoxal phosphate By similarity
Binding site1901Pyridoxal phosphate By similarity
Binding site2241Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2161N6-(pyridoxal phosphate)lysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q9LR29 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 4B5FEA35566BBD12

FASTA38844,064
        10         20         30         40         50         60 
MMVGCENSKK SDSGSNEDKS LSDDIINLDQ GDPTAFQEYW MKKKDRCTVV IPAWDLMSYF 

        70         80         90        100        110        120 
SDTKNVCWFL EPELEKAIKA LHGAIGNAAT EERYIVVGTG SSQLCQAALF ALSSLSEVKP 

       130        140        150        160        170        180 
VSIVAAVPYY STYVEEASYL QSTLYKWEGD ARTFDKKGPY IELVTSPNNP DGIMREPVVN 

       190        200        210        220        230        240 
RREGGKVIHD LAYYWPHYTP ITRRQDHDLM LFTFSKITGH AGSRIGWALV KDIEVAKKMV 

       250        260        270        280        290        300 
HYLTINSIGV SKESQTRATT ILNELTKTCR TQSESFFEYG YEKMKSRWER LREVVESGDA 

       310        320        330        340        350        360 
FTLPNYPQDF CNFFGKTLST SPAFAWLGYK EERDLGSLLK EKKVLTRGGD RCGCNKRYVR 

       370        380 
VSMLSRDDDF DVSLQRLATI KDLKCVEP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"TAA1-mediated auxin biosynthesis is essential for hormone crosstalk and plant development."
Stepanova A.N., Robertson-Hoyt J., Yun J., Benavente L.M., Xie D.Y., Dolezal K., Schlereth A., Juergens G., Alonso J.M.
Cell 133:177-191(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY ETHYLENE, GENE FAMILY, NOMENCLATURE.
[4]"Rapid synthesis of auxin via a new tryptophan-dependent pathway is required for shade avoidance in plants."
Tao Y., Ferrer J.L., Ljung K., Pojer F., Hong F., Long J.A., Li L., Moreno J.E., Bowman M.E., Ivans L.J., Cheng Y., Lim J., Zhao Y., Ballare C.L., Sandberg G., Noel J.P., Chory J.
Cell 133:164-176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[5]"A small-molecule screen identifies L-kynurenine as a competitive inhibitor of TAA1/TAR activity in ethylene-directed auxin biosynthesis and root growth in Arabidopsis."
He W., Brumos J., Li H., Ji Y., Ke M., Gong X., Zeng Q., Li W., Zhang X., An F., Wen X., Li P., Chu J., Sun X., Yan C., Yan N., Xie D.Y., Raikhel N. expand/collapse author list , Yang Z., Stepanova A.N., Alonso J.M., Guo H.
Plant Cell 23:3944-3960(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC005292 Genomic DNA. Translation: AAF87014.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE30372.1.
RefSeqNP_173746.1. NM_102181.1.
UniGeneAt.51734.

3D structure databases

ProteinModelPortalQ9LR29.
SMRQ9LR29. Positions 21-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G23320.1-P.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G23320.1; AT1G23320.1; AT1G23320.
GeneID838941.
KEGGath:AT1G23320.

Organism-specific databases

TAIRAT1G23320.

Phylogenomic databases

eggNOGNOG284125.
HOGENOMHOG000237549.
InParanoidQ9LR29.
KOK16903.
OMACENSKKS.
ProtClustDBCLSN2682072.

Enzyme and pathway databases

UniPathwayUPA00151.

Gene expression databases

GenevestigatorQ9LR29.

Family and domain databases

Gene3D2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF04864. Alliinase_C. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTAR1_ARATH
AccessionPrimary (citable) accession number: Q9LR29
Secondary accession number(s): F4I655
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 66 of the entry and version 2 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