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Q8NS38 (TYSY_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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
Ordered Locus Names:Cgl0844, cg0966
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00008.

Sequence similarities

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

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Cellular componentCytoplasm
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
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 – 266266Thymidylate synthase HAMAP-Rule MF_00008
PRO_0000140952

Sites

Active site1491 By similarity

Secondary structure

.......................................... 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8NS38 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: E63BA3445460DF09

FASTA26630,230
        10         20         30         40         50         60 
MTVPTPYEDL LRKIAEEGSH KDDRTGTGTT SLFGQQIRFD LNEGFPLLTT KKVHFHSVVG 

        70         80         90        100        110        120 
ELLWFLQGDS NVKWLQDNNI RIWNEWADED GELGPVYGVQ WRSWPTPDGR HIDQISGALE 

       130        140        150        160        170        180 
TLRNNPDSRR NIVSAWNVSE LENMALPPCH LLFQLYVADG KLSCQLYQRS ADMFLGVPFN 

       190        200        210        220        230        240 
IASYALLTHM FAQQAGLEVG EFIWTGGDCH IYDNHKEQVA EQLSREARPY PTLELNKAAS 

       250        260 
MFEYSFDDIT VSGYDPHPLI RGKVAV 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB98237.1.
BX927150 Genomic DNA. Translation: CAF19550.1.
RefSeqNP_600073.1. NC_003450.3.
YP_225136.1. NC_006958.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4H0RX-ray2.30A/B1-266[»]
4H0UX-ray2.75A/B/C/D1-266[»]
ProteinModelPortalQ8NS38.
SMRQ8NS38. Positions 7-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg0966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98237; BAB98237; BAB98237.
CAF19550; CAF19550; cg0966.
GeneID1018839.
KEGGcgb:cg0966.
cgl:NCgl0810.
PATRIC21493738. VBICorGlu203724_0828.

Phylogenomic databases

eggNOGCOG0207.
HOGENOMHOG000257899.
KOK00560.
OMAFGRQIRY.
OrthoDBEOG6K6V53.

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. 2 hits.
PROSITEPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTYSY_CORGL
AccessionPrimary (citable) accession number: Q8NS38
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 79 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