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Q8RXU4 (THA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable low-specificity L-threonine aldolase 1

EC=4.1.2.48
Alternative name(s):
Threonine aldolase 1
Gene names
Name:THA1
Ordered Locus Names:At1g08630
ORF Names:F22O13.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Threonine aldolase involved in threonine degradation to glycine. May play a role in the removal of L-allo-threonine. Ref.7 Ref.8

Catalytic activity

L-threonine = glycine + acetaldehyde.

L-allo-threonine = glycine + acetaldehyde.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid degradation; L-threonine degradation via aldolase pathway; acetaldehyde and glycine from L-threonine: step 1/1.

Tissue specificity

Expressed in root tips, seedlings, carpels and seeds. Ref.8

Disruption phenotype

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. Ref.8

Sequence similarities

Belongs to the threonine aldolase family.

Biophysicochemical properties

Kinetic parameters:

KM=7.1 mM for L-threonine Ref.7

Sequence caution

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

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processthreonine catabolic process

Inferred from mutant phenotype Ref.8. Source: TAIR

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

threonine aldolase activity

Inferred from direct assay Ref.8. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8RXU4-1)

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.
Isoform 2 (identifier: Q8RXU4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     270-283: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Probable low-specificity L-threonine aldolase 1
PRO_0000428659

Amino acid modifications

Modified residue2071N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence270 – 28314Missing in isoform 2.
VSP_054082

Experimental info

Mutagenesis1141G → R in tha1-1; loss of function; 50-fold increase in seed Thr content and 2-fold decrease in seedling Gly content. Ref.7 Ref.8
Sequence conflict3211N → K in AAM63785. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E38254B11A967514

FASTA35838,942
        10         20         30         40         50         60 
MVMRSVDLRS DTVTRPTDAM REAMCNAEVD DDVLGYDPTA RRLEEEMAKM MGKEAALFVP 

        70         80         90        100        110        120 
SGTMGNLISV MVHCDVRGSE VILGDNCHIH VYENGGISTI GGVHPKTVKN EEDGTMDLEA 

       130        140        150        160        170        180 
IEAAIRDPKG STFYPSTRLI CLENTHANSG GRCLSVEYTE KVGEIAKRHG VKLHIDGARL 

       190        200        210        220        230        240 
FNASIALGVP VHKLVKAADS VQVCLSKGLG APVGSVIVGS QSFIEKAKTV RKTLGGGMRQ 

       250        260        270        280        290        300 
IGVLCAAALV ALQENLPKLQ HDHKKAKLLA EGLNQMKGIR VNVAAVETNM IFMDMEDGSR 

       310        320        330        340        350 
LTAEKLRKNL EENGILLIRG NSSRIRIVIH HQITTSDVHY TLSCFQQAML TMQEPSRT 

« Hide

Isoform 2 [UniParc].

Checksum: 3541C1DA6F33C8CA
Show »

FASTA34437,431

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]"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] (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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT00716.
RefSeqNP_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]
UniGeneAt.57057.

3D structure databases

ProteinModelPortalQ8RXU4.
SMRQ8RXU4. Positions 6-347.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G08630.1; 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]
GeneID837385.
KEGGath:AT1G08630.

Organism-specific databases

TAIRAT1G08630.

Phylogenomic databases

InParanoidQ8RXU4.
KOK01620.
OMAEVGDEQI.
PhylomeDBQ8RXU4.

Enzyme and pathway databases

BioCycARA:GQT-1115-MONOMER.
ARA:GQT-1116-MONOMER.
ARA:GQT-1117-MONOMER.
ARA:GQT-1118-MONOMER.
BRENDA2.1.2.1. 302.
UniPathwayUPA00044; UER00429.

Gene expression databases

ArrayExpressQ8RXU4.
GenevestigatorQ8RXU4.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR001597. 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]
PfamPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHA1_ARATH
AccessionPrimary (citable) accession number: Q8RXU4
Secondary accession number(s): B9DG61 expand/collapse secondary AC list , Q2V4P5, Q8LC88, Q9FRS2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 90 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