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Protein

L-tryptophan--pyruvate aminotransferase 1

Gene

TAA1

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

Functioni

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.4 Publications

Catalytic activityi

L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate.1 Publication
L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine.1 Publication

Cofactori

Enzyme regulationi

Inhibited by L-kynurenine.1 Publication

Kineticsi

  1. KM=0.29 mM for L-tryptophan1 Publication
  2. KM=4.74 mM for tyrosine1 Publication
  3. KM=9.35 mM for phenylalanine1 Publication
  1. Vmax=25.8 µmol/min/µg enzyme with L-tryptophan as substrate1 Publication
  2. Vmax=28 µmol/min/µg enzyme with tyrosine as substrate1 Publication
  3. Vmax=10.6 µmol/min/µg enzyme with phenylalanine as substrate1 Publication

pH dependencei

Optimum pH is 8.8.1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius.1 Publication

Pathwayi: auxin biosynthesis

This protein is involved in the pathway auxin biosynthesis, which is part of Plant hormone metabolism.
View all proteins of this organism that are known to be involved in the pathway auxin biosynthesis and in Plant hormone metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei58Pyridoxal phosphate1
Binding sitei168Pyridoxal phosphate1
Binding sitei191Pyridoxal phosphate1
Binding sitei225Pyridoxal phosphate1

GO - Molecular functioni

  • carbon-sulfur lyase activity Source: InterPro
  • L-alanine:2-oxoglutarate aminotransferase activity Source: TAIR
  • L-glutamine:2-oxoglutarate aminotransferase activity Source: TAIR
  • L-leucine:2-oxoglutarate aminotransferase activity Source: TAIR
  • L-methionine:2-oxoglutarate aminotransferase activity Source: TAIR
  • L-phenylalanine:2-oxoglutarate aminotransferase activity Source: TAIR
  • L-phenylalanine:pyruvate aminotransferase activity Source: TAIR
  • L-tryptophan:2-oxoglutarate aminotransferase activity Source: TAIR
  • L-tryptophan:pyruvate aminotransferase activity Source: TAIR
  • L-tyrosine:2-oxoglutarate aminotransferase activity Source: TAIR
  • L-tyrosine:pyruvate aminotransferase activity Source: TAIR
  • pyridoxal phosphate binding Source: TAIR

GO - Biological processi

  • defense response to bacterium Source: TAIR
  • flower development Source: TAIR
  • gynoecium development Source: TAIR
  • indoleacetic acid biosynthetic process Source: TAIR
  • leaf development Source: TAIR
  • maintenance of root meristem identity Source: TAIR
  • phloem or xylem histogenesis Source: TAIR
  • positive gravitropism Source: TAIR
  • response to ethylene Source: TAIR
  • root development Source: TAIR
  • shade avoidance Source: TAIR
  • shoot system development Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Auxin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:AT1G70560-MONOMER.
MetaCyc:AT1G70560-MONOMER.
BRENDAi2.6.1.27. 399.
2.6.1.99. 399.
UniPathwayiUPA00151.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TAA1
Synonyms:CKRC1, SAV3, TIR2, WEI8
Ordered Locus Names:At1g70560
ORF Names:F24J13.13, F5A18.26
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G70560.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi166P → S in wei8-2; loss of activity. 1 Publication1
Mutagenesisi171G → E in tir2-1; loss of activity. 1 Publication1
Mutagenesisi217K → A: Loss of activity. 2 Publications1
Mutagenesisi217K → G or R: Reduces growth rate under shade condition. 2 Publications1
Mutagenesisi250G → S in sav3-3; reduces growth rate under shade condition. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004013751 – 391L-tryptophan--pyruvate aminotransferase 1Add BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei217N6-(pyridoxal phosphate)lysineSequence analysis1

Proteomic databases

PaxDbiQ9S7N2.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

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.2 Publications

Inductioni

Up-regulated by trans-zeatin, ethylene and high temperature. Down-regulated by auxin and shade treatment.3 Publications

Gene expression databases

GenevisibleiQ9S7N2. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G70560.1.

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni20 – 22Combined sources3
Helixi33 – 35Combined sources3
Helixi36 – 41Combined sources6
Helixi43 – 45Combined sources3
Beta strandi48 – 50Combined sources3
Turni52 – 55Combined sources4
Beta strandi64 – 66Combined sources3
Helixi71 – 84Combined sources14
Beta strandi90 – 98Combined sources9
Helixi99 – 113Combined sources15
Beta strandi115 – 124Combined sources10
Helixi131 – 137Combined sources7
Beta strandi144 – 150Combined sources7
Beta strandi159 – 166Combined sources8
Turni168 – 170Combined sources3
Beta strandi187 – 191Combined sources5
Turni197 – 199Combined sources3
Beta strandi209 – 214Combined sources6
Helixi215 – 219Combined sources5
Helixi222 – 224Combined sources3
Beta strandi226 – 231Combined sources6
Helixi234 – 248Combined sources15
Helixi253 – 269Combined sources17
Turni275 – 277Combined sources3
Helixi279 – 299Combined sources21
Beta strandi302 – 305Combined sources4
Beta strandi312 – 314Combined sources3
Turni315 – 318Combined sources4
Beta strandi319 – 321Combined sources3
Beta strandi326 – 335Combined sources10
Helixi338 – 344Combined sources7
Helixi352 – 355Combined sources4
Beta strandi361 – 366Combined sources6
Helixi370 – 381Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BWNX-ray2.25A/B/C/D/E/F1-391[»]
3BWOX-ray2.40A/B/C/D/E/F1-391[»]
ProteinModelPortaliQ9S7N2.
SMRiQ9S7N2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9S7N2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni100 – 101Pyridoxal phosphate binding2
Regioni191 – 194Pyridoxal phosphate binding4
Regioni214 – 217Pyridoxal phosphate binding4

Sequence similaritiesi

Belongs to the alliinase family.Curated

Phylogenomic databases

eggNOGiENOG410II7N. Eukaryota.
ENOG41114NM. LUCA.
HOGENOMiHOG000237549.
InParanoidiQ9S7N2.
KOiK16903.
OMAiWEGDAWG.
OrthoDBiEOG09360BJJ.
PhylomeDBiQ9S7N2.

Family and domain databases

Gene3Di2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF04864. Alliinase_C. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9S7N2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLENSRKP EKISNKNIPM SDFVVNLDHG DPTAYEEYWR KMGDRCTVTI
60 70 80 90 100
RGCDLMSYFS DMTNLCWFLE PELEDAIKDL HGVVGNAATE DRYIVVGTGS
110 120 130 140 150
TQLCQAAVHA LSSLARSQPV SVVAAAPFYS TYVEETTYVR SGMYKWEGDA
160 170 180 190 200
WGFDKKGPYI ELVTSPNNPD GTIRETVVNR PDDDEAKVIH DFAYYWPHYT
210 220 230 240 250
PITRRQDHDI MLFTFSKITG HAGSRIGWAL VKDKEVAKKM VEYIIVNSIG
260 270 280 290 300
VSKESQVRTA KILNVLKETC KSESESENFF KYGREMMKNR WEKLREVVKE
310 320 330 340 350
SDAFTLPKYP EAFCNYFGKS LESYPAFAWL GTKEETDLVS ELRRHKVMSR
360 370 380 390
AGERCGSDKK HVRVSMLSRE DVFNVFLERL ANMKLIKSID L
Length:391
Mass (Da):44,801
Last modified:May 1, 2000 - v1
Checksum:i7038D6C93E122614
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF96729.
RefSeqiNP_177213.1. NM_105724.3.
UniGeneiAt.27817.

Genome annotation databases

EnsemblPlantsiAT1G70560.1; AT1G70560.1; AT1G70560.
GeneIDi843393.
GrameneiAT1G70560.1; AT1G70560.1; AT1G70560.
KEGGiath:AT1G70560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF96729.
RefSeqiNP_177213.1. NM_105724.3.
UniGeneiAt.27817.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BWNX-ray2.25A/B/C/D/E/F1-391[»]
3BWOX-ray2.40A/B/C/D/E/F1-391[»]
ProteinModelPortaliQ9S7N2.
SMRiQ9S7N2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G70560.1.

Proteomic databases

PaxDbiQ9S7N2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G70560.1; AT1G70560.1; AT1G70560.
GeneIDi843393.
GrameneiAT1G70560.1; AT1G70560.1; AT1G70560.
KEGGiath:AT1G70560.

Organism-specific databases

TAIRiAT1G70560.

Phylogenomic databases

eggNOGiENOG410II7N. Eukaryota.
ENOG41114NM. LUCA.
HOGENOMiHOG000237549.
InParanoidiQ9S7N2.
KOiK16903.
OMAiWEGDAWG.
OrthoDBiEOG09360BJJ.
PhylomeDBiQ9S7N2.

Enzyme and pathway databases

UniPathwayiUPA00151.
BioCyciARA:AT1G70560-MONOMER.
MetaCyc:AT1G70560-MONOMER.
BRENDAi2.6.1.27. 399.
2.6.1.99. 399.

Miscellaneous databases

EvolutionaryTraceiQ9S7N2.
PROiQ9S7N2.

Gene expression databases

GenevisibleiQ9S7N2. AT.

Family and domain databases

Gene3Di2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF04864. Alliinase_C. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTAA1_ARATH
AccessioniPrimary (citable) accession number: Q9S7N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.