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Q9MT28 (THRC_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Threonine synthase, chloroplastic

Short name=TS
EC=4.2.3.1
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine By similarity.

Catalytic activity

O-phospho-L-homoserine + H2O = L-threonine + phosphate.

Cofactor

Pyridoxal phosphate By similarity.

Enzyme regulation

Allosterically activated by S-adenosyl-methionine (SAM) By similarity.

Pathway

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast By similarity.

Sequence similarities

Belongs to the threonine synthase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Threonine biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandPyridoxal phosphate
S-adenosyl-L-methionine
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processthreonine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

threonine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Chloroplast By similarity
Chain41 – 519479Threonine synthase, chloroplastic
PRO_0000033618

Regions

Region328 – 3325Pyridoxal phosphate binding By similarity

Sites

Binding site4651Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1961N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9MT28 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 114C0979CD231464

FASTA51957,412
        10         20         30         40         50         60 
MAASCMLRSS FISPGLPQLH HQSTSKPNNG IHFFTPIKAT ATNDAISQQK HRRPADENIR 

        70         80         90        100        110        120 
EEARRHCSSH NFSARYVPFN AGPNSDEWYS LDEIVYRSRS GGLLDVQHDM DALKKFDGQY 

       130        140        150        160        170        180 
WRSLFDSRVG KTTWPYGSGV WSKKEWVLPE IDSDDIVSAF EGNSNLFWAE RFGKQFLGMT 

       190        200        210        220        230        240 
DLWVKHCGIS HTGSFKDLGM TVLVSQVNRL RKMHKPVVGV GCASTGDTSA ALSAYCASAG 

       250        260        270        280        290        300 
IPSIVFLPAN KISMAQLVQP IANGAFVLSI DTDFDGCMQL IREVTAELPI YLANSLNSLR 

       310        320        330        340        350        360 
LEGQKTAAIE ILQQFDWEVP EWVIVPGGNL GNIYAFYKGF QMCKELGLVD RIPRLVCAQA 

       370        380        390        400        410        420 
ANANPLYLHY KSGWKDFKPV KANTTFASAI QIGDPVSIDR AVFALQQCNG IVEEATEEEL 

       430        440        450        460        470        480 
MDAMAQADST GMFICPHTGV ALTALFKLRN SGVIAPTDRT VVVSTAHGLK FTQSKIDYHS 

       490        500        510 
KEIKDMECRF ANPPVEVKAD FGSVMDVLKS YLLSQNSKL 

« Hide

References

[1]"Expression of threonine synthase from Solanum tuberosum L. is not metabolically regulated by photosynthesis-related signals or by nitrogenous compounds."
Casazza A.P., Basner A., Hoefgen R., Hesse H.
Plant Sci. 157:43-50(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF082894 mRNA. Translation: AAF74984.1.
RefSeqNP_001274994.1. NM_001288065.1.
UniGeneStu.478.

3D structure databases

ProteinModelPortalQ9MT28.
SMRQ9MT28. Positions 48-517.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102577745.
KEGGsot:102577745.

Phylogenomic databases

KOK01733.

Enzyme and pathway databases

UniPathwayUPA00050; UER00065.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHRC_SOLTU
AccessionPrimary (citable) accession number: Q9MT28
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 61 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