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Protein

Threonine synthase

Gene

thrc

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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

Pathway: L-threonine biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-threonine from L-aspartate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Probable aspartokinase (SPBC19F5.04)
  2. Probable aspartate-semialdehyde dehydrogenase (SPCC1827.06c)
  3. Probable homoserine dehydrogenase (SPBC776.03)
  4. Probable homoserine kinase (SPBC4C3.03)
  5. Threonine synthase (thrc)
This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Threonine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase (EC:4.2.3.1)
Short name:
TS
Gene namesi
Name:thrc
ORF Names:SPAC9E9.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC9E9.06c.
PomBaseiSPAC9E9.06c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Threonine synthasePRO_0000185644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei321 – 3211Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ42598.
PaxDbiQ42598.

Interactioni

Protein-protein interaction databases

MINTiMINT-4700437.
STRINGi4896.SPAC9E9.06c.1.

Structurei

3D structure databases

ProteinModelPortaliQ42598.
SMRiQ42598. Positions 2-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Phylogenomic databases

eggNOGiCOG0498.
HOGENOMiHOG000230745.
InParanoidiQ42598.
KOiK01733.
OMAiNVHALAI.
OrthoDBiEOG7N0CDH.
PhylomeDBiQ42598.

Family and domain databases

Gene3Di3.90.1380.10. 1 hit.
InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q42598-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQVSYLST RGGSSNFSFE EAVLKGLAND GGLFIPSEIP QLPSGWIEAW
60 70 80 90 100
KDKSFPEIAF EVMSLYIPRS EISADELKKL VDRSYSTFRH PETTPLKSLK
110 120 130 140 150
NGLNVLELFH GPTFAFKDVA LQFLGNLFEF FLTRKNGNKP EDERDHLTVV
160 170 180 190 200
GATSGDTGSA AIYGLRGKKD VSVFILFPNG RVSPIQEAQM TTVTDPNVHC
210 220 230 240 250
ITVNGVFDDC QDLVKQIFGD VEFNKKHHIG AVNSINWARI LSQITYYLYS
260 270 280 290 300
YLSVYKQGKA DDVRFIVPTG NFGDILAGYY AKRMGLPTKQ LVIATNENDI
310 320 330 340 350
LNRFFKTGRY EKADSTQVSP SGPISAKETY SPAMDILVSS NFERYLWYLA
360 370 380 390 400
LATEAPNHTP AEASEILSRW MNEFKRDGTV TVRPEVLEAA RRDFVSERVS
410 420 430 440 450
NDETIDAIKK IYESDHYIID PHTAVGVETG LRCLEKTKDQ DITYICLSTA
460 470 480 490 500
HPAKFDKAVN LALSSYSDYN FNTQVLPIEF DGLLDEERTC IFSGKPNIDI
510
LKQIIEVTLS REKA
Length:514
Mass (Da):57,632
Last modified:November 1, 1996 - v1
Checksum:i1C61AEFBB5F961C4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2542SV → PA in BAA13852 (PubMed:9501991).Curated
Sequence conflicti446 – 4461C → W in BAA13852 (PubMed:9501991).Curated
Sequence conflicti456 – 4561D → G in BAA13852 (PubMed:9501991).Curated
Sequence conflicti459 – 4591V → G in BAA13852 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46263 mRNA. Translation: CAA86405.1.
CU329670 Genomic DNA. Translation: CAB16415.1.
D89190 mRNA. Translation: BAA13852.1.
PIRiT39213.
T42748.
RefSeqiNP_594579.1. NM_001020008.2.

Genome annotation databases

EnsemblFungiiSPAC9E9.06c.1; SPAC9E9.06c.1:pep; SPAC9E9.06c.
GeneIDi2542653.
KEGGispo:SPAC9E9.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46263 mRNA. Translation: CAA86405.1.
CU329670 Genomic DNA. Translation: CAB16415.1.
D89190 mRNA. Translation: BAA13852.1.
PIRiT39213.
T42748.
RefSeqiNP_594579.1. NM_001020008.2.

3D structure databases

ProteinModelPortaliQ42598.
SMRiQ42598. Positions 2-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4700437.
STRINGi4896.SPAC9E9.06c.1.

Proteomic databases

MaxQBiQ42598.
PaxDbiQ42598.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC9E9.06c.1; SPAC9E9.06c.1:pep; SPAC9E9.06c.
GeneIDi2542653.
KEGGispo:SPAC9E9.06c.

Organism-specific databases

EuPathDBiFungiDB:SPAC9E9.06c.
PomBaseiSPAC9E9.06c.

Phylogenomic databases

eggNOGiCOG0498.
HOGENOMiHOG000230745.
InParanoidiQ42598.
KOiK01733.
OMAiNVHALAI.
OrthoDBiEOG7N0CDH.
PhylomeDBiQ42598.

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.

Miscellaneous databases

NextBioi20803702.
PROiQ42598.

Family and domain databases

Gene3Di3.90.1380.10. 1 hit.
InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of cDNA encoding threonine synthase from Schizosaccharomyces pombe by functional expression in Saccharomyces cerevisiae."
    Aas S.F., Rognes S.E.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-514.
    Strain: PR745.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTHRC_SCHPO
AccessioniPrimary (citable) accession number: Q42598
Secondary accession number(s): P78841
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Was originally (Ref. 1) thought to originate from A.thaliana.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.