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Protein

Threonine synthase, chloroplastic

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei465 – 4651Pyridoxal phosphateBy similarity

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. threonine synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. threonine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Threonine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase, chloroplastic (EC:4.2.3.1)
Short name:
TS
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115: Unplaced

Subcellular locationi

Plastidchloroplast By similarity

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040ChloroplastBy similarityAdd
BLAST
Chaini41 – 519479Threonine synthase, chloroplasticPRO_0000033618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961N6-(pyridoxal phosphate)lysineBy similarity

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9MT28.
SMRiQ9MT28. Positions 48-517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni328 – 3325Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK01733.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9MT28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASCMLRSS FISPGLPQLH HQSTSKPNNG IHFFTPIKAT ATNDAISQQK
60 70 80 90 100
HRRPADENIR EEARRHCSSH NFSARYVPFN AGPNSDEWYS LDEIVYRSRS
110 120 130 140 150
GGLLDVQHDM DALKKFDGQY WRSLFDSRVG KTTWPYGSGV WSKKEWVLPE
160 170 180 190 200
IDSDDIVSAF EGNSNLFWAE RFGKQFLGMT DLWVKHCGIS HTGSFKDLGM
210 220 230 240 250
TVLVSQVNRL RKMHKPVVGV GCASTGDTSA ALSAYCASAG IPSIVFLPAN
260 270 280 290 300
KISMAQLVQP IANGAFVLSI DTDFDGCMQL IREVTAELPI YLANSLNSLR
310 320 330 340 350
LEGQKTAAIE ILQQFDWEVP EWVIVPGGNL GNIYAFYKGF QMCKELGLVD
360 370 380 390 400
RIPRLVCAQA ANANPLYLHY KSGWKDFKPV KANTTFASAI QIGDPVSIDR
410 420 430 440 450
AVFALQQCNG IVEEATEEEL MDAMAQADST GMFICPHTGV ALTALFKLRN
460 470 480 490 500
SGVIAPTDRT VVVSTAHGLK FTQSKIDYHS KEIKDMECRF ANPPVEVKAD
510
FGSVMDVLKS YLLSQNSKL
Length:519
Mass (Da):57,412
Last modified:October 1, 2000 - v1
Checksum:i114C0979CD231464
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082894 mRNA. Translation: AAF74984.1.
RefSeqiNP_001274994.1. NM_001288065.1.
UniGeneiStu.478.

Genome annotation databases

GeneIDi102577745.
KEGGisot:102577745.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082894 mRNA. Translation: AAF74984.1.
RefSeqiNP_001274994.1. NM_001288065.1.
UniGeneiStu.478.

3D structure databases

ProteinModelPortaliQ9MT28.
SMRiQ9MT28. Positions 48-517.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102577745.
KEGGisot:102577745.

Phylogenomic databases

KOiK01733.

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiTHRC_SOLTU
AccessioniPrimary (citable) accession number: Q9MT28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 65 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

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.