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P13100 (TYSY_PNECA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Thymidylate synthase

Short name=TS
Short name=TSase
EC=2.1.1.45
Gene names
Name:THYA
OrganismPneumocystis carinii
Taxonomic identifier4754 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008

Pathway

Pyrimidine metabolism; dTTP biosynthesis. HAMAP-Rule MF_00008

Subunit structure

Homodimer.

Sequence similarities

Belongs to the thymidylate synthase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processdTMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

dTTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionthymidylate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Thymidylate synthase HAMAP-Rule MF_00008
PRO_0000140911

Sites

Active site1731

Secondary structure

.................................................. 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13100 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 985F6F870EF2A7B2

FASTA29734,362
        10         20         30         40         50         60 
MVNAEEQQYL NLVQYIINHG EDRPDRTGTG TLSVFAPSPL KFSLRNKTFP LLTTKRVFIR 

        70         80         90        100        110        120 
GVIEELLWFI RGETDSLKLR EKNIHIWDAN GSREYLDSIG LTKRQEGDLG PIYGFQWRHF 

       130        140        150        160        170        180 
GAEYIDCKTN YIGQGVDQLA NIIQKIRTSP YDRRLILSAW NPADLEKMAL PPCHMFCQFY 

       190        200        210        220        230        240 
VHIPSNNHRP ELSCQLYQRS CDMGLGVPFN IASYALLTCM IAHVCDLDPG DFIHVMGDCH 

       250        260        270        280        290 
IYKDHIEALQ QQLTRSPRPF PTLSLNRSIT DIEDFTLDDF NIQNYHPYET IKMKMSI 

« Hide

References

[1]"Isolation and expression of the Pneumocystis carinii thymidylate synthase gene."
Edman U., Edman J.C., Lundgren B., Santi D.V.
Proc. Natl. Acad. Sci. U.S.A. 86:6503-6507(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Polymorphism of the thymidylate synthase gene of Pneumocystis carinii from different host species."
Mazars E., Odberg-Ferragut C., Dei-Cas E., Fourmaux M.N., Aliouat E.M., Brun-Pascaud M., Mougeot G., Camus D.
J. Eukaryot. Microbiol. 42:26-32(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-210.
[3]"The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits."
Anderson A.C., O'Neil R.H., DeLano W.L., Stroud R.M.
Biochemistry 38:13829-13836(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25415 Genomic DNA. Translation: AAA33802.1.
S77510 Genomic DNA. Translation: AAB34157.1.
PIRYXUNTP. A33720.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI7X-ray2.60A/B1-297[»]
1F28X-ray1.90A/B/C/D1-297[»]
ProteinModelPortalP13100.
SMRP13100. Positions 3-297.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP13100.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00575.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
HAMAPMF_00008. Thymidy_synth_bact.
InterProIPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSPR00108. THYMDSNTHASE.
SUPFAMSSF55831. SSF55831. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13100.

Entry information

Entry nameTYSY_PNECA
AccessionPrimary (citable) accession number: P13100
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: February 19, 2014
This is version 84 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways