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P00469 (TYSY_LACCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 109. 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
OrganismLactobacillus casei
Taxonomic identifier1582 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Provides the sole de novo source of dTMP for DNA biosynthesis. HAMAP-Rule MF_00008

Catalytic activity

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

Pathway

Pyrimidine metabolism; dTTP biosynthesis. HAMAP-Rule MF_00008

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00008.

Sequence similarities

Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.

Sequence caution

The sequence AAA25255.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Cellular componentCytoplasm
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processdTMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

dTTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionthymidylate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Thymidylate synthase HAMAP-Rule MF_00008
PRO_0000140967

Sites

Active site1981

Secondary structure

............................................................ 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00469 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 4C391722044FF0A5

FASTA31636,580
        10         20         30         40         50         60 
MLEQPYLDLA KKVLDEGHFK PDRTHTGTYS IFGHQMRFDL SKGFPLLTTK KVPFGLIKSE 

        70         80         90        100        110        120 
LLWFLHGDTN IRFLLQHRNH IWDEWAFEKW VKSDEYHGPD MTDFGHRSQK DPEFAAVYHE 

       130        140        150        160        170        180 
EMAKFDDRVL HDDAFAAKYG DLGLVYGSQW RAWHTSKGDT IDQLGDVIEQ IKTHPYSRRL 

       190        200        210        220        230        240 
IVSAWNPEDV PTMALPPCHT LYQFYVNDGK LSLQLYQRSA DIFLGVPFNI ASYALLTHLV 

       250        260        270        280        290        300 
AHECGLEVGE FIHTFGDAHL YVNHLDQIKE QLSRTPRPAP TLQLNPDKHD IFDFDMKDIK 

       310 
LLNYDPYPAI KAPVAV 

« Hide

References

[1]"Cloning, sequencing, and expression of the Lactobacillus casei thymidylate synthase gene."
Pinter K., Davisson V.J., Santi D.V.
DNA 7:235-241(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The primary structure of Lactobacillus casei thymidylate synthetase. III. The use of 2-(2-nitrophenylsulfenyl)-3-methyl-3-bromoindolenine and limited tryptic peptides to establish the complete amino acid sequence of the enzyme."
Maley G.F., Bellisario R.L., Guarino D.U., Maley F.
J. Biol. Chem. 254:1301-1304(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases."
Perry K.M., Fauman E.B., Finer-Moore J.S., Montfort W.R., Maley G.F., Maley F., Stroud R.M.
Proteins 8:315-333(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
[4]"Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei."
Finer-Moore J.S., Fauman E.B., Foster P.G., Perry K.M., Santi D.V., Stroud R.M.
J. Mol. Biol. 232:1101-1116(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
[5]"Role of the conserved tryptophan 82 of Lactobacillus casei thymidylate synthase."
Kealey J.T., Eckstein J., Santi D.V.
Chem. Biol. 2:609-614(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-82.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19653 Genomic DNA. Translation: AAA25255.1. Different initiation.
PIRSYLBT. A29817.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BO7X-ray2.40A1-316[»]
1BO8X-ray2.40A1-316[»]
1BP0X-ray2.40A1-316[»]
1BP6X-ray2.40A1-316[»]
1BPJX-ray2.40A1-316[»]
1JMFX-ray2.50A1-316[»]
1JMGX-ray2.20A1-316[»]
1JMHX-ray2.50A1-316[»]
1JMIX-ray2.50A1-316[»]
1LCAX-ray2.50A1-316[»]
1LCBX-ray2.50A1-316[»]
1LCEX-ray2.50A1-316[»]
1NJAX-ray2.50A1-316[»]
1NJBX-ray2.74A1-316[»]
1NJCX-ray2.50A1-316[»]
1NJDX-ray2.20A1-316[»]
1NJEX-ray2.30A1-316[»]
1TDAX-ray3.09A1-315[»]
1TDBX-ray2.65A1-315[»]
1TDCX-ray2.65A1-315[»]
1THYX-ray2.90A1-316[»]
1TSLX-ray2.50A1-316[»]
1TSMX-ray3.00A1-316[»]
1TSVX-ray2.90A1-316[»]
1TSWX-ray2.50A1-316[»]
1TSXX-ray2.50A1-316[»]
1TSYX-ray2.20A1-316[»]
1TSZX-ray2.75A1-316[»]
1TVUX-ray2.50A1-316[»]
1TVVX-ray2.30A1-316[»]
1TVWX-ray2.50A1-316[»]
1VZAX-ray2.50A1-316[»]
1VZBX-ray2.50A1-316[»]
1VZCX-ray2.50A1-316[»]
1VZDX-ray2.50A1-316[»]
1VZEX-ray2.30A1-316[»]
2G86X-ray2.40A1-316[»]
2G89X-ray2.50A1-316[»]
2G8AX-ray2.40A1-316[»]
2G8DX-ray2.40A1-316[»]
2TDDX-ray2.70A1-315[»]
2TDMX-ray2.55A1-316[»]
3BNZX-ray2.60A1-316[»]
3BYXX-ray2.40A1-316[»]
3BZ0X-ray2.70A1-316[»]
3C06X-ray2.60A1-316[»]
3C0AX-ray2.40A1-316[»]
3IJZX-ray2.21A1-316[»]
3IK0X-ray2.10A1-316[»]
3IK1X-ray2.25A1-316[»]
4TMSX-ray2.35A1-316[»]
ProteinModelPortalP00469.
SMRP00469. Positions 1-316.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00469.
ChEMBLCHEMBL5328.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00469.
UniPathwayUPA00575.

Family and domain databases

Gene3D3.30.572.10. 2 hits.
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

EvolutionaryTraceP00469.

Entry information

Entry nameTYSY_LACCA
AccessionPrimary (citable) accession number: P00469
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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