Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9S7N2 (TAA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
L-tryptophan--pyruvate aminotransferase 1

EC=2.6.1.27
EC=2.6.1.99
Alternative name(s):
Protein CYTOKININ INDUCED ROOT CURLING 1
Protein SHADE AVOIDANCE 3
Protein TRANSPORT INHIBITOR RESPONSE 2
Protein TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS 1
Protein WEAK ETHYLENE INSENSITIVE 8
Tryptophan transaminase
Gene names
Name:TAA1
Synonyms:CKRC1, SAV3, TIR2, WEI8
Ordered Locus Names:At1g70560
ORF Names:F24J13.13, F5A18.26
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

L-tryptophan aminotransferase involved in auxin (IAA) biosynthesis. Can convert L-tryptophan and pyruvate to indole-3-pyruvic acid (IPA) and alanine. Catalyzes the first step in IPA branch of the auxin biosynthetic pathway. Required for auxin production to initiate multiple change in growth in response to environmental and developmental cues. It is also active with phenylalanine, tyrosine, leucine, alanine, methionine and glutamine. Both TAA1 and TAR2 are required for maintaining proper auxin levels in roots, while TAA1, TAR1 and TAR2 are required for proper embryo patterning. Involved in the maintenance of the root stem cell niches and required for shade avoidance. Ref.5 Ref.6 Ref.7 Ref.10

Catalytic activity

L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate. Ref.10

L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine. Ref.10

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Inhibited by L-kynurenine. Ref.8

Pathway

Plant hormone metabolism; auxin biosynthesis.

Subcellular location

Cytoplasm Ref.6.

Tissue specificity

Expressed at the leaf margin and in the vasculature of emerging young leaves. Expressed in the quiescent center and in the vasculature of root tips. Detected in the shoot apical meristem, stems, sepals, stamen filaments, the shoot and root junction, the stigma and the base of the silique. Ref.6 Ref.7 Ref.9

Developmental stage

In the heart stage embryo, expressed in the developing vasculature and the apical epidermal layer. At the torpedo stage expressed in the developing vasculature of the root, hypocotyl and cotyledons, as well as in the L1 layer of the presumptive shoot apical meristem and the adaxial epidermis of the developing cotyledons. In flowers, the expression is first restricted to the central outer layers of flower primordia, but later expands toward the base of gynoecia, becoming limited to two cell files along the meristematic medial ridge. Ref.6 Ref.7

Induction

Up-regulated by trans-zeatin, ethylene and high temperature. Down-regulated by auxin and shade treatment. Ref.6 Ref.7 Ref.8 Ref.9

Disruption phenotype

No visible phenotype under normal growth condition, but exhibits reduced levels of auxin (IAA), reduced auxin response, reduced sensitivity to ethylene and shorter hypocotyls and petioles but larger leaf area when grown in simulated shade. Defective in root gravitropic response and shows an increased resistance to cytokinin in primary root growth. Ref.5 Ref.6 Ref.7 Ref.9

Sequence similarities

Belongs to the alliinase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.29 mM for L-tryptophan Ref.6

KM=4.74 mM for tyrosine

KM=9.35 mM for phenylalanine

Vmax=25.8 µmol/min/µg enzyme with L-tryptophan as substrate

Vmax=28 µmol/min/µg enzyme with tyrosine as substrate

Vmax=10.6 µmol/min/µg enzyme with phenylalanine as substrate

pH dependence:

Optimum pH is 8.8.

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

Ontologies

Keywords
   Biological processAuxin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcotyledon development

Inferred from genetic interaction Ref.5. Source: TAIR

cotyledon vascular tissue pattern formation

Inferred from genetic interaction Ref.5. Source: TAIR

defense response to bacterium

Inferred from genetic interaction PubMed 22181713. Source: TAIR

embryo development ending in seed dormancy

Inferred from genetic interaction Ref.5. Source: TAIR

flower development

Inferred from genetic interaction Ref.5. Source: TAIR

gynoecium development

Inferred from genetic interaction Ref.5. Source: TAIR

indoleacetic acid biosynthetic process

Inferred from mutant phenotype Ref.6. Source: TAIR

leaf development

Inferred from mutant phenotype Ref.6. Source: TAIR

maintenance of root meristem identity

Inferred from genetic interaction Ref.5. Source: TAIR

phloem or xylem histogenesis

Inferred from genetic interaction Ref.5. Source: TAIR

positive gravitropism

Inferred from mutant phenotype Ref.5. Source: TAIR

primary root development

Inferred from genetic interaction Ref.5. Source: TAIR

response to ethylene

Inferred from mutant phenotype Ref.5. Source: TAIR

root development

Inferred from mutant phenotype Ref.5. Source: TAIR

shade avoidance

Inferred from mutant phenotype Ref.6. Source: TAIR

shoot system development

Inferred from genetic interaction Ref.5. Source: TAIR

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: TAIR

   Molecular_functionL-alanine:2-oxoglutarate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-glutamine:2-oxoglutarate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-leucine:2-oxoglutarate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-methionine:2-oxoglutarate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-phenylalanine:2-oxoglutarate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-phenylalanine:pyruvate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-tryptophan:2-oxoglutarate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-tryptophan:pyruvate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-tyrosine:2-oxoglutarate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

L-tyrosine:pyruvate aminotransferase activity

Inferred from direct assay Ref.6. Source: TAIR

carbon-sulfur lyase activity

Inferred from electronic annotation. Source: InterPro

pyridoxal phosphate binding

Inferred from direct assay Ref.6. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391L-tryptophan--pyruvate aminotransferase 1
PRO_0000401375

Regions

Region100 – 1012Pyridoxal phosphate binding
Region191 – 1944Pyridoxal phosphate binding
Region214 – 2174Pyridoxal phosphate binding

Sites

Binding site581Pyridoxal phosphate
Binding site1681Pyridoxal phosphate
Binding site1911Pyridoxal phosphate
Binding site2251Pyridoxal phosphate

Amino acid modifications

Modified residue2171N6-(pyridoxal phosphate)lysine Potential

Experimental info

Mutagenesis1661P → S in wei8-2; loss of activity. Ref.5
Mutagenesis1711G → E in tir2-1; loss of activity. Ref.7
Mutagenesis2171K → A: Loss of activity. Ref.5 Ref.6
Mutagenesis2171K → G or R: Reduces growth rate under shade condition. Ref.5 Ref.6
Mutagenesis2501G → S in sav3-3; reduces growth rate under shade condition. Ref.6

Secondary structure

................................................................ 391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9S7N2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7038D6C93E122614

FASTA39144,801
        10         20         30         40         50         60 
MVKLENSRKP EKISNKNIPM SDFVVNLDHG DPTAYEEYWR KMGDRCTVTI RGCDLMSYFS 

        70         80         90        100        110        120 
DMTNLCWFLE PELEDAIKDL HGVVGNAATE DRYIVVGTGS TQLCQAAVHA LSSLARSQPV 

       130        140        150        160        170        180 
SVVAAAPFYS TYVEETTYVR SGMYKWEGDA WGFDKKGPYI ELVTSPNNPD GTIRETVVNR 

       190        200        210        220        230        240 
PDDDEAKVIH DFAYYWPHYT PITRRQDHDI MLFTFSKITG HAGSRIGWAL VKDKEVAKKM 

       250        260        270        280        290        300 
VEYIIVNSIG VSKESQVRTA KILNVLKETC KSESESENFF KYGREMMKNR WEKLREVVKE 

       310        320        330        340        350        360 
SDAFTLPKYP EAFCNYFGKS LESYPAFAWL GTKEETDLVS ELRRHKVMSR AGERCGSDKK 

       370        380        390 
HVRVSMLSRE DVFNVFLERL ANMKLIKSID L 

« 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]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]"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, MUTAGENESIS OF PRO-166 AND LYS-217.
[6]"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: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PYRIDOXAMINE PHOSPHATE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY SHADE, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-217 AND GLY-250.
[7]"The TRANSPORT INHIBITOR RESPONSE2 gene is required for auxin synthesis and diverse aspects of plant development."
Yamada M., Greenham K., Prigge M.J., Jensen P.J., Estelle M.
Plant Physiol. 151:168-179(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-171, TISSUE SPECIFICITY, INDUCTION BY AUXIN AND HEAT, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[8]"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.
[9]"Functional characterization of the CKRC1/TAA1 gene and dissection of hormonal actions in the Arabidopsis root."
Zhou Z.Y., Zhang C.G., Wu L., Zhang C.G., Chai J., Wang M., Jha A., Jia P.F., Cui S.J., Yang M., Chen R., Guo G.Q.
Plant J. 66:516-527(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY ETHYLENE AND CYTOKININ, DISRUPTION PHENOTYPE.
[10]"The main auxin biosynthesis pathway in Arabidopsis."
Mashiguchi K., Tanaka K., Sakai T., Sugawara S., Kawaide H., Natsume M., Hanada A., Yaeno T., Shirasu K., Yao H., McSteen P., Zhao Y., Hayashi K., Kamiya Y., Kasahara H.
Proc. Natl. Acad. Sci. U.S.A. 108:18512-18517(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC010796 Genomic DNA. Translation: AAG52476.1.
AC011663 Genomic DNA. Translation: AAG52348.1.
CP002684 Genomic DNA. Translation: AEE35079.1.
AK117208 mRNA. Translation: BAC41884.1.
BT005339 mRNA. Translation: AAO63403.1.
PIRF96729.
RefSeqNP_177213.1. NM_105724.2.
UniGeneAt.27817.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BWNX-ray2.25A/B/C/D/E/F1-391[»]
3BWOX-ray2.40A/B/C/D/E/F1-391[»]
ProteinModelPortalQ9S7N2.
SMRQ9S7N2. Positions 17-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G70560.1-P.

Proteomic databases

PaxDbQ9S7N2.
PRIDEQ9S7N2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G70560.1; AT1G70560.1; AT1G70560.
GeneID843393.
KEGGath:AT1G70560.

Organism-specific databases

TAIRAT1G70560.

Phylogenomic databases

eggNOGNOG300354.
HOGENOMHOG000237549.
InParanoidQ9S7N2.
KOK16903.
OMACDLMSYF.
PhylomeDBQ9S7N2.

Enzyme and pathway databases

BioCycARA:AT1G70560-MONOMER.
MetaCyc:AT1G70560-MONOMER.
UniPathwayUPA00151.

Gene expression databases

GenevestigatorQ9S7N2.

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...

Other

EvolutionaryTraceQ9S7N2.

Entry information

Entry nameTAA1_ARATH
AccessionPrimary (citable) accession number: Q9S7N2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 81 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names