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P11044 (TYSY2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. 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
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 2
Short name=TS 2
Short name=TSase 2
EC=2.1.1.45
Alternative name(s):
Thymidylate synthase B
Short name=TS B
Short name=TSase B
Gene names
Name:thyA2
Synonyms:thyB
Ordered Locus Names:BSU21820
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length264 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 By similarity.

Miscellaneous

B.subtilis strain 168 possesses two thymidylate synthases, a major form ThyA and a minor form ThyB. HAMAP-Rule MF_00008

Sequence similarities

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

Biophysicochemical properties

Temperature dependence:

Thermolabile. Inactive at 46 degrees Celsius. HAMAP-Rule MF_00008

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Cellular componentCytoplasm
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdTMP biosynthetic process

Inferred from electronic annotation. Source: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Thymidylate synthase 2 HAMAP-Rule MF_00008
PRO_0000140932

Sites

Active site1461

Natural variations

Natural variant71F → L in strain: ATCC 6633.
Natural variant371N → H in strain: ATCC 6633.
Natural variant391R → Q in strain: ATCC 6633.
Natural variant1871I → M in strain: ATCC 6633.
Natural variant2211E → T in strain: ATCC 6633.
Natural variant2241V → L in strain: ATCC 6633.
Natural variant2291Q → K in strain: ATCC 6633.
Natural variant235 – 2362KV → EI in strain: ATCC 6633.

Sequences

Sequence LengthMass (Da)Tools
P11044 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 1BFE1F1BD8202E64

FASTA26430,538
        10         20         30         40         50         60 
MKQYKDFCRH VLEHGEKKGD RTGTGTISTF GYQMRFNLRE GFPMLTTKKL HFKSIAHELL 

        70         80         90        100        110        120 
WFLKGDTNVR YLQENGVRIW NEWADENGEL GPVYGSQWRS WRGADGETID QISRLIEDIK 

       130        140        150        160        170        180 
TNPNSRRLIV SAWNVGEIDK MALPPCHCLF QFYVSDGKLS CQLYQRSADV FLGVPFNIAS 

       190        200        210        220        230        240 
YALLTMIIAH VTGLEPGEFI HTFGDVHIYQ NHIEQVNLQL ERDVRPLPQL RFARKVDSIF 

       250        260 
NFAFEDFIIE DYDPHPHIKG AVSV

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the thymidylate synthase B and dihydrofolate reductase genes contained in one Bacillus subtilis operon."
Iwakura M., Kawata M., Tsuda K., Tanaka T.
Gene 64:9-20(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Organization of the Bacillus subtilis 168 chromosome between kdg and the attachment site of the SP beta prophage: use of long accurate PCR and yeast artificial chromosomes for sequencing."
Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.
Microbiology 142:3005-3015(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[3]"Heat-stable and heat-labile thymidylate synthases B of Bacillus subtilis: comparison of the nucleotide and amino acid sequences."
Montorsi M., Lorenzetti R.
Mol. Gen. Genet. 239:1-5(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 and ATCC 6633 / PCI 219 / NRS 231.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X69661 Genomic DNA. Translation: CAA49350.1.
L77246 Genomic DNA. Translation: AAA96634.1.
M20012 Genomic DNA. Translation: AAA22852.1.
AL009126 Genomic DNA. Translation: CAB14100.1.
PIRSYBSTB. JT0290.
S35239.
RefSeqNP_390065.1. NC_000964.3.

3D structure databases

ProteinModelPortalP11044.
SMRP11044. Positions 1-250.
ModBaseSearch...

Protein-protein interaction databases

IntActP11044. 4 interactions.
STRING224308.BSU21820.

Proteomic databases

PaxDbP11044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14100; CAB14100; BSU21820.
GeneID939092.
KEGGbsu:BSU21820.
PATRIC18976169. VBIBacSub10457_2275.

Organism-specific databases

GenoListBSU21820. [Micado]

Phylogenomic databases

eggNOGCOG0207.
HOGENOMHOG000257899.
KOK00560.
OMADTNVAYL.
ProtClustDBPRK01827.

Enzyme and pathway databases

BioCycBSUB:BSU21820-MONOMER.
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. Thymidylat_synth_C. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 2 hits.
PROSITEPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTYSY2_BACSU
AccessionPrimary (citable) accession number: P11044
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents