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Q00063 (THRC_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 90. 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

Short name=TS
EC=4.2.3.1
Gene names
Name:THR4
Ordered Locus Names:AAR059C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Sequence similarities

Belongs to the threonine synthase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Threonine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processthreonine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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

Chain1 – 512512Threonine synthase
PRO_0000185643

Amino acid modifications

Modified residue1211N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q00063 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E527C4E449881671

FASTA51258,925
        10         20         30         40         50         60 
MSQVYRSTRS SSEDTKSFEE AVIQGLAEDG GLFLPAVIPR LREETLFEHW AHLSFQDLAM 

        70         80         90        100        110        120 
EIMKFYIADW EIPAPELREL IERSYSSFRS EEVTPLRKNV TGDDENLHIL ELFHGPTYAF 

       130        140        150        160        170        180 
KDVALQFVGN LFEYFLERKN RDVSEEERTH LTVVGATSGD TGSAAIYGLR GKQDVSVFIL 

       190        200        210        220        230        240 
YPHGRISPIQ EEQMTTVEDE NVHTMAIEGS FDNCQDIVKS IFVDEEFNRK HNIAAVNSIN 

       250        260        270        280        290        300 
WARILAQITY YFYSYFRATD GQPGRVKFIV PSGNFGDILA GFYAKQMGLP IEKLVIATNE 

       310        320        330        340        350        360 
NDILDRFLRE GVYERSEDVT ATHSPAMDIL VSSNFERLLW FFAREQLAQG DDQEAGSIVN 

       370        380        390        400        410        420 
RWFEQLREER RFDVPEHLLD AIRYHFDSER VDNYNTLASI RHIYEHAQNP ERYVIDPHTA 

       430        440        450        460        470        480 
VGICAANRQI AHDQNNEIHY ISLATAHPAK FADAVNEALS SYDDYNFDDV LPDRLRRLGD 

       490        500        510 
LEKRIKYVDN TDVDVIKSII EEELINMGIY NP 

« Hide

References

« Hide 'large scale' references
[1]"AgTHR4, a new selection marker for transformation of the filamentous fungus Ashbya gossypii, maps in a four-gene cluster that is conserved between A. gossypii and Saccharomyces cerevisiae."
Altmann-Joehl R., Philippsen P.
Mol. Gen. Genet. 250:69-80(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[3]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91046 Genomic DNA. Translation: CAA62506.1.
AE016814 Genomic DNA. Translation: AAS50424.1.
PIRS61905.
RefSeqNP_982600.1. NM_207953.1.

3D structure databases

ProteinModelPortalQ00063.
SMRQ00063. Positions 2-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_AAR059C.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS50424; AAS50424; AGOS_AAR059C.
GeneID4618427.
KEGGago:AGOS_AAR059C.

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000230745.
KOK01733.
OMAEEIASWA.
OrthoDBEOG7N0CDH.
PhylomeDBQ00063.

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_ASHGO
AccessionPrimary (citable) accession number: Q00063
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways