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Q9MT28

- THRC_SOLTU

UniProt

Q9MT28 - THRC_SOLTU

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Protein
Threonine synthase, chloroplastic
Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - 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

Pyridoxal phosphate By similarity.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei465 – 4651Pyridoxal phosphate By 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 – 4040Chloroplast By similarity
Add
BLAST
Chaini41 – 519479Threonine synthase, chloroplastic
PRO_0000033618Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9MT28.
SMRiQ9MT28. Positions 48-517.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK01733.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[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

MAASCMLRSS FISPGLPQLH HQSTSKPNNG IHFFTPIKAT ATNDAISQQK    50
HRRPADENIR EEARRHCSSH NFSARYVPFN AGPNSDEWYS LDEIVYRSRS 100
GGLLDVQHDM DALKKFDGQY WRSLFDSRVG KTTWPYGSGV WSKKEWVLPE 150
IDSDDIVSAF EGNSNLFWAE RFGKQFLGMT DLWVKHCGIS HTGSFKDLGM 200
TVLVSQVNRL RKMHKPVVGV GCASTGDTSA ALSAYCASAG IPSIVFLPAN 250
KISMAQLVQP IANGAFVLSI DTDFDGCMQL IREVTAELPI YLANSLNSLR 300
LEGQKTAAIE ILQQFDWEVP EWVIVPGGNL GNIYAFYKGF QMCKELGLVD 350
RIPRLVCAQA ANANPLYLHY KSGWKDFKPV KANTTFASAI QIGDPVSIDR 400
AVFALQQCNG IVEEATEEEL MDAMAQADST GMFICPHTGV ALTALFKLRN 450
SGVIAPTDRT VVVSTAHGLK FTQSKIDYHS KEIKDMECRF ANPPVEVKAD 500
FGSVMDVLKS YLLSQNSKL 519
Length:519
Mass (Da):57,412
Last modified:October 1, 2000 - v1
Checksum:i114C0979CD231464
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF082894 mRNA. Translation: AAF74984.1 .
RefSeqi NP_001274994.1. NM_001288065.1.
UniGenei Stu.478.

3D structure databases

ProteinModelPortali Q9MT28.
SMRi Q9MT28. Positions 48-517.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 102577745.
KEGGi sot:102577745.

Phylogenomic databases

KOi K01733.

Enzyme and pathway databases

UniPathwayi UPA00050 ; UER00065 .

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR00260. thrC. 1 hit.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 61 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

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