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Protein

Thymidylate synthase 2

Gene

thyA2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Provides the sole de novo source of dTMP for DNA biosynthesis.

Catalytic activityi

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.UniRule annotation

Temperature dependencei

Thermolabile. Inactive at 46 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei146 – 1461

GO - Molecular functioni

  1. thymidylate synthase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. dTMP biosynthetic process Source: UniProtKB-HAMAP
  2. dTTP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU21820-MONOMER.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthase 2UniRule annotation (EC:2.1.1.45UniRule annotation)
Short name:
TS 2UniRule annotation
Short name:
TSase 2UniRule annotation
Alternative name(s):
Thymidylate synthase BUniRule annotation
Short name:
TS BUniRule annotation
Short name:
TSase BUniRule annotation
Gene namesi
Name:thyA2UniRule annotation
Synonyms:thyB
Ordered Locus Names:BSU21820
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU21820. [Micado]

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Thymidylate synthase 2PRO_0000140932Add
BLAST

Proteomic databases

PaxDbiP11044.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP11044. 6 interactions.
STRINGi224308.BSU21820.

Structurei

3D structure databases

ProteinModelPortaliP11044.
SMRiP11044. Positions 1-250.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0207.
HOGENOMiHOG000257899.
InParanoidiP11044.
KOiK00560.
OMAiNEWADEN.
OrthoDBiEOG6K6V53.
PhylomeDBiP11044.

Family and domain databases

Gene3Di3.30.572.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact.
InterProiIPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamiPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 2 hits.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11044-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKQYKDFCRH VLEHGEKKGD RTGTGTISTF GYQMRFNLRE GFPMLTTKKL
60 70 80 90 100
HFKSIAHELL WFLKGDTNVR YLQENGVRIW NEWADENGEL GPVYGSQWRS
110 120 130 140 150
WRGADGETID QISRLIEDIK TNPNSRRLIV SAWNVGEIDK MALPPCHCLF
160 170 180 190 200
QFYVSDGKLS CQLYQRSADV FLGVPFNIAS YALLTMIIAH VTGLEPGEFI
210 220 230 240 250
HTFGDVHIYQ NHIEQVNLQL ERDVRPLPQL RFARKVDSIF NFAFEDFIIE
260
DYDPHPHIKG AVSV
Length:264
Mass (Da):30,538
Last modified:July 1, 1989 - v1
Checksum:i1BFE1F1BD8202E64
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71F → L in strain: ATCC 6633.
Natural varianti37 – 371N → H in strain: ATCC 6633.
Natural varianti39 – 391R → Q in strain: ATCC 6633.
Natural varianti187 – 1871I → M in strain: ATCC 6633.
Natural varianti221 – 2211E → T in strain: ATCC 6633.
Natural varianti224 – 2241V → L in strain: ATCC 6633.
Natural varianti229 – 2291Q → K in strain: ATCC 6633.
Natural varianti235 – 2362KV → EI in strain: ATCC 6633.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69661 Genomic DNA. Translation: CAA49350.1.
L77246 Genomic DNA. Translation: AAA96634.1.
M20012 Genomic DNA. Translation: AAA22852.1.
AL009126 Genomic DNA. Translation: CAB14100.1.
PIRiJT0290. SYBSTB.
S35239.
RefSeqiNP_390065.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14100; CAB14100; BSU21820.
GeneIDi939092.
KEGGibsu:BSU21820.
PATRICi18976169. VBIBacSub10457_2275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69661 Genomic DNA. Translation: CAA49350.1.
L77246 Genomic DNA. Translation: AAA96634.1.
M20012 Genomic DNA. Translation: AAA22852.1.
AL009126 Genomic DNA. Translation: CAB14100.1.
PIRiJT0290. SYBSTB.
S35239.
RefSeqiNP_390065.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP11044.
SMRiP11044. Positions 1-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11044. 6 interactions.
STRINGi224308.BSU21820.

Proteomic databases

PaxDbiP11044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14100; CAB14100; BSU21820.
GeneIDi939092.
KEGGibsu:BSU21820.
PATRICi18976169. VBIBacSub10457_2275.

Organism-specific databases

GenoListiBSU21820. [Micado]

Phylogenomic databases

eggNOGiCOG0207.
HOGENOMiHOG000257899.
InParanoidiP11044.
KOiK00560.
OMAiNEWADEN.
OrthoDBiEOG6K6V53.
PhylomeDBiP11044.

Enzyme and pathway databases

UniPathwayiUPA00575.
BioCyciBSUB:BSU21820-MONOMER.

Family and domain databases

Gene3Di3.30.572.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact.
InterProiIPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamiPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 2 hits.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTYSY2_BACSU
AccessioniPrimary (citable) accession number: P11044
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.