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Q8RXU4

- THA1_ARATH

UniProt

Q8RXU4 - THA1_ARATH

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Protein

Probable low-specificity L-threonine aldolase 1

Gene

THA1

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

Functioni

Threonine aldolase involved in threonine degradation to glycine. May play a role in the removal of L-allo-threonine.2 Publications

Catalytic activityi

L-threonine = glycine + acetaldehyde.
L-allo-threonine = glycine + acetaldehyde.

Cofactori

Pyridoxal phosphate.By similarity

Kineticsi

  1. KM=7.1 mM for L-threonine1 Publication

Pathwayi

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. threonine aldolase activity Source: TAIR

GO - Biological processi

  1. threonine catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:GQT-1115-MONOMER.
ARA:GQT-1116-MONOMER.
ARA:GQT-1117-MONOMER.
ARA:GQT-1118-MONOMER.
BRENDAi2.1.2.1. 302.
UniPathwayiUPA00044; UER00429.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable low-specificity L-threonine aldolase 1 (EC:4.1.2.48)
Alternative name(s):
Threonine aldolase 1
Gene namesi
Name:THA1
Ordered Locus Names:At1g08630
ORF Names:F22O13.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G08630.

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but mutant plants have 50-fold increase in seed Thr content and 2-fold decrease in seedling Gly content.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141G → R in tha1-1; loss of function; 50-fold increase in seed Thr content and 2-fold decrease in seedling Gly content. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Probable low-specificity L-threonine aldolase 1PRO_0000428659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei207 – 2071N6-(pyridoxal phosphate)lysineBy similarity

Expressioni

Tissue specificityi

Expressed in root tips, seedlings, carpels and seeds.1 Publication

Gene expression databases

ExpressionAtlasiQ8RXU4. baseline and differential.
GenevestigatoriQ8RXU4.

Structurei

3D structure databases

ProteinModelPortaliQ8RXU4.
SMRiQ8RXU4. Positions 6-347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the threonine aldolase family.Curated

Phylogenomic databases

InParanoidiQ8RXU4.
KOiK01620.
OMAiEVGDEQI.
PhylomeDBiQ8RXU4.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8RXU4-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVMRSVDLRS DTVTRPTDAM REAMCNAEVD DDVLGYDPTA RRLEEEMAKM
60 70 80 90 100
MGKEAALFVP SGTMGNLISV MVHCDVRGSE VILGDNCHIH VYENGGISTI
110 120 130 140 150
GGVHPKTVKN EEDGTMDLEA IEAAIRDPKG STFYPSTRLI CLENTHANSG
160 170 180 190 200
GRCLSVEYTE KVGEIAKRHG VKLHIDGARL FNASIALGVP VHKLVKAADS
210 220 230 240 250
VQVCLSKGLG APVGSVIVGS QSFIEKAKTV RKTLGGGMRQ IGVLCAAALV
260 270 280 290 300
ALQENLPKLQ HDHKKAKLLA EGLNQMKGIR VNVAAVETNM IFMDMEDGSR
310 320 330 340 350
LTAEKLRKNL EENGILLIRG NSSRIRIVIH HQITTSDVHY TLSCFQQAML

TMQEPSRT
Length:358
Mass (Da):38,942
Last modified:June 1, 2002 - v1
Checksum:iE38254B11A967514
GO
Isoform 2 (identifier: Q8RXU4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     270-283: Missing.

Note: No experimental confirmation available.

Show »
Length:344
Mass (Da):37,431
Checksum:i3541C1DA6F33C8CA
GO

Sequence cautioni

The sequence AAF99780.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti321 – 3211N → K in AAM63785. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei270 – 28314Missing in isoform 2. 1 PublicationVSP_054082Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC003981 Genomic DNA. Translation: AAF99780.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28320.1.
CP002684 Genomic DNA. Translation: AEE28321.1.
CP002684 Genomic DNA. Translation: AEE28322.1.
CP002684 Genomic DNA. Translation: AEE28323.1.
CP002684 Genomic DNA. Translation: AEE28324.1.
AY080670 mRNA. Translation: AAL86346.1.
AY117227 mRNA. Translation: AAM51302.1.
AK317034 mRNA. Translation: BAH19728.1.
AK230078 mRNA. Translation: BAF01898.1.
AY086734 mRNA. Translation: AAM63785.1.
PIRiT00716.
RefSeqiNP_001031001.2. NM_001035924.2. [Q8RXU4-1]
NP_001077492.1. NM_001084023.1. [Q8RXU4-2]
NP_563822.1. NM_100736.2. [Q8RXU4-1]
NP_849614.1. NM_179283.2. [Q8RXU4-1]
NP_849615.1. NM_179284.3. [Q8RXU4-1]
UniGeneiAt.57057.

Genome annotation databases

EnsemblPlantsiAT1G08630.1; AT1G08630.1; AT1G08630. [Q8RXU4-1]
AT1G08630.2; AT1G08630.2; AT1G08630. [Q8RXU4-1]
AT1G08630.3; AT1G08630.3; AT1G08630. [Q8RXU4-1]
AT1G08630.4; AT1G08630.4; AT1G08630. [Q8RXU4-1]
AT1G08630.5; AT1G08630.5; AT1G08630. [Q8RXU4-2]
GeneIDi837385.
KEGGiath:AT1G08630.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC003981 Genomic DNA. Translation: AAF99780.1 . Sequence problems.
CP002684 Genomic DNA. Translation: AEE28320.1 .
CP002684 Genomic DNA. Translation: AEE28321.1 .
CP002684 Genomic DNA. Translation: AEE28322.1 .
CP002684 Genomic DNA. Translation: AEE28323.1 .
CP002684 Genomic DNA. Translation: AEE28324.1 .
AY080670 mRNA. Translation: AAL86346.1 .
AY117227 mRNA. Translation: AAM51302.1 .
AK317034 mRNA. Translation: BAH19728.1 .
AK230078 mRNA. Translation: BAF01898.1 .
AY086734 mRNA. Translation: AAM63785.1 .
PIRi T00716.
RefSeqi NP_001031001.2. NM_001035924.2. [Q8RXU4-1 ]
NP_001077492.1. NM_001084023.1. [Q8RXU4-2 ]
NP_563822.1. NM_100736.2. [Q8RXU4-1 ]
NP_849614.1. NM_179283.2. [Q8RXU4-1 ]
NP_849615.1. NM_179284.3. [Q8RXU4-1 ]
UniGenei At.57057.

3D structure databases

ProteinModelPortali Q8RXU4.
SMRi Q8RXU4. Positions 6-347.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G08630.1 ; AT1G08630.1 ; AT1G08630 . [Q8RXU4-1 ]
AT1G08630.2 ; AT1G08630.2 ; AT1G08630 . [Q8RXU4-1 ]
AT1G08630.3 ; AT1G08630.3 ; AT1G08630 . [Q8RXU4-1 ]
AT1G08630.4 ; AT1G08630.4 ; AT1G08630 . [Q8RXU4-1 ]
AT1G08630.5 ; AT1G08630.5 ; AT1G08630 . [Q8RXU4-2 ]
GeneIDi 837385.
KEGGi ath:AT1G08630.

Organism-specific databases

TAIRi AT1G08630.

Phylogenomic databases

InParanoidi Q8RXU4.
KOi K01620.
OMAi EVGDEQI.
PhylomeDBi Q8RXU4.

Enzyme and pathway databases

UniPathwayi UPA00044 ; UER00429 .
BioCyci ARA:GQT-1115-MONOMER.
ARA:GQT-1116-MONOMER.
ARA:GQT-1117-MONOMER.
ARA:GQT-1118-MONOMER.
BRENDAi 2.1.2.1. 302.

Gene expression databases

ExpressionAtlasi Q8RXU4. baseline and differential.
Genevestigatori Q8RXU4.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view ]
Pfami PF01212. Beta_elim_lyase. 1 hit.
[Graphical view ]
PIRSFi PIRSF017617. Thr_aldolase. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "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] (ISOFORM 1).
    Strain: cv. Columbia.
  4. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "Application of a high-throughput HPLC-MS/MS assay to Arabidopsis mutant screening; evidence that threonine aldolase plays a role in seed nutritional quality."
    Jander G., Norris S.R., Joshi V., Fraga M., Rugg A., Yu S., Li L., Last R.L.
    Plant J. 39:465-475(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-114.
  8. "Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool."
    Joshi V., Laubengayer K.M., Schauer N., Fernie A.R., Jander G.
    Plant Cell 18:3564-3575(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-114.

Entry informationi

Entry nameiTHA1_ARATH
AccessioniPrimary (citable) accession number: Q8RXU4
Secondary accession number(s): B9DG61
, Q2V4P5, Q8LC88, Q9FRS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: June 1, 2002
Last modified: October 29, 2014
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

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