Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A7GP90 (TYSY_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:
Thymidylate synthase

Short name=TS
Short name=TSase
EC=2.1.1.45
Gene names
Name:thyA
Ordered Locus Names:Bcer98_1639
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 termComplete 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 – 318318Thymidylate synthase HAMAP-Rule MF_00008
PRO_1000073867

Sites

Active site2001 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GP90 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: CD855B461136241F

FASTA31836,810
        10         20         30         40         50         60 
MKHAEYEYLN LCRHVMEHGT KKEDRTGTGT VSVFGYQMRF DLSKGFPLLT TKRVPFRLVA 

        70         80         90        100        110        120 
SELLWFMKGD TNIRYLLQHN NNIWNEWAFK NWVESDEYKG PDMTNFGLRS QEDEAFKTQY 

       130        140        150        160        170        180 
DEQMEIFKKN VLEDDEFARK YGYLGDVYGK QWRAWKTAAG ETIDQLKDVI EMIKKTPDSR 

       190        200        210        220        230        240 
RLIVSAWNPE DVPNMALPPC HTLFQFYVAD GKLSCQLYQR SGDIFLGIPF NIASYSLLTH 

       250        260        270        280        290        300 
LIAHECGLAV GEFVHTIGDA HIYTNHFEQV KKQLAREPRP FPTLKLNSDV KSVFDFEMGD 

       310 
LTIEGYDPHP AIKAPVAV 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS21948.1.
RefSeqYP_001374943.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GP90.
SMRA7GP90. Positions 5-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315749.Bcer98_1639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS21948; ABS21948; Bcer98_1639.
GeneID5347186.
KEGGbcy:Bcer98_1639.
PATRIC18931750. VBIBacCyt128034_1719.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0207.
HOGENOMHOG000257899.
KOK00560.
OMAAQWRHWE.
OrthoDBEOG6K6V53.

Enzyme and pathway databases

BioCycBCYT315749:GH2A-1752-MONOMER.
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...

Entry information

Entry nameTYSY_BACCN
AccessionPrimary (citable) accession number: A7GP90
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 49 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

PATHWAY comments

Index of metabolic and biosynthesis pathways