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P16120 (THRC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonine synthase
Short name=TS
EC=4.2.3.1
Gene names
Name:THR4
Ordered Locus Names:YCR053W
ORF Names:YCR53W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Pathway

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

Miscellaneous

Present with 26000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the threonine synthase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SSM4P403181EBI-19259,EBI-18208

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Threonine synthase
PRO_0000185645

Amino acid modifications

Modified residue1241N6-(pyridoxal phosphate)lysine By similarity
Modified residue4671Phosphoserine Ref.7
Modified residue4691Phosphotyrosine Ref.7
Modified residue4701Phosphoserine Ref.7

Experimental info

Sequence conflict1761K → R in AAU09679. Ref.5

Secondary structure

1 ............................................................................. 514
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16120 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: EF6BA9DF56D94B6F

FASTA51457,474
        10         20         30         40         50         60 
MPNASQVYRS TRSSSPKTIS FEEAIIQGLA TDGGLFIPPT IPQVDQATLF NDWSKLSFQD 

        70         80         90        100        110        120 
LAFAIMRLYI AQEEIPDADL KDLIKRSYST FRSDEVTPLV QNVTGDKENL HILELFHGPT 

       130        140        150        160        170        180 
YAFKDVALQF VGNLFEYFLQ RTNANLPEGE KKQITVVGAT SGDTGSAAIY GLRGKKDVSV 

       190        200        210        220        230        240 
FILYPTGRIS PIQEEQMTTV PDENVQTLSV TGTFDNCQDI VKAIFGDKEF NSKHNVGAVN 

       250        260        270        280        290        300 
SINWARILAQ MTYYFYSFFQ ATNGKDSKKV KFVVPSGNFG DILAGYFAKK MGLPIEKLAI 

       310        320        330        340        350        360 
ATNENDILDR FLKSGLYERS DKVAATLSPA MDILISSNFE RLLWYLAREY LANGDDLKAG 

       370        380        390        400        410        420 
EIVNNWFQEL KTNGKFQVDK SIIEGASKDF TSERVSNEET SETIKKIYES SVNPKHYILD 

       430        440        450        460        470        480 
PHTAVGVCAT ERLIAKDNDK SIQYISLSTA HPAKFADAVN NALSGFSNYS FEKDVLPEEL 

       490        500        510 
KKLSTLKKKL KFIERADVEL VKNAIEEELA KMKL

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the yeast THR4 gene encoding threonine synthase."
Aas S.F., Rognes S.E.
Nucleic Acids Res. 18:665-665(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26786 / X2180-1A.
[2]"Analysis of the THR4 region on chromosome III of the yeast Saccharomyces cerevisiae."
Mannhaupt G., van der Linden C.G., Vetter I., Maurer K., Pilz U., Planta R.J., Feldmann H.
Yeast 6:353-361(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; TYR-469 AND SER-470, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X17256 Genomic DNA. Translation: CAA35157.1.
X59720 Genomic DNA. Translation: CAA42284.1.
AY723762 Genomic DNA. Translation: AAU09679.1.
BK006937 Genomic DNA. Translation: DAA07530.1.
PIRSYBSR. S22836.
RefSeqNP_009982.1. NM_001178767.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KL7X-ray2.70A/B1-514[»]
ProteinModelPortalP16120.
SMRP16120. Positions 2-512.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6522N.
IntActP16120. 5 interactions.
MINTMINT-2787019.
STRING4932.YCR053W.

Proteomic databases

PaxDbP16120.
PeptideAtlasP16120.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR053W; YCR053W; YCR053W.
GeneID850420.
KEGGsce:YCR053W.

Organism-specific databases

CYGDYCR053w.
SGDS000000649. THR4.

Phylogenomic databases

eggNOGCOG0498.
GeneTreeENSGT00530000063879.
HOGENOMHOG000230745.
KOK01733.
OMAEEIASWA.
OrthoDBEOG43V33W.

Enzyme and pathway databases

UniPathwayUPA00050; UER00065.

Gene expression databases

GenevestigatorP16120.
GermOnlineYCR053W. Saccharomyces cerevisiae.

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. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16120.
NextBio965986.

Entry information

Entry nameTHRC_YEAST
AccessionPrimary (citable) accession number: P16120
Secondary accession number(s): D6VR61, E9P943
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 3, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents