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Protein

Thymidylate synthase 1

Gene

thyA1

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.UniRule annotation

Catalytic activityi

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

Temperature dependencei

Thermostable. Active at 46 degrees Celsius.

Pathwayi: dTTP biosynthesis

This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway dTTP biosynthesis and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei161NucleophileUniRule annotation1
Binding sitei1845,10-methylenetetrahydrofolateUniRule annotation1
Binding sitei192dUMPUniRule annotation1
Binding sitei2785,10-methylenetetrahydrofolate; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi141 – 142dUMP; shared with dimeric partnerUniRule annotation2
Nucleotide bindingi181 – 184dUMPUniRule annotation4
Nucleotide bindingi222 – 224dUMPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

BRENDAi2.1.1.45. 658.
SABIO-RKP0CI79.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthase 1UniRule annotation (EC:2.1.1.45UniRule annotation)
Short name:
TS 1UniRule annotation
Short name:
TSase 1UniRule annotation
Alternative name(s):
Thymidylate synthase A1 Publication
Short name:
TS A1 Publication
Short name:
TSase A1 Publication
Gene namesi
Name:thyA1UniRule annotation
Ordered Locus Names:BSU17680
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001409311 – 279Thymidylate synthase 1Add BLAST279

Proteomic databases

PaxDbiP0CI79.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009726.

Structurei

Secondary structure

1279
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 18Combined sources15
Helixi22 – 24Combined sources3
Turni32 – 34Combined sources3
Beta strandi40 – 50Combined sources11
Beta strandi52 – 54Combined sources3
Beta strandi59 – 61Combined sources3
Helixi65 – 76Combined sources12
Helixi83 – 87Combined sources5
Turni88 – 90Combined sources3
Helixi95 – 97Combined sources3
Beta strandi100 – 103Combined sources4
Beta strandi105 – 107Combined sources3
Helixi109 – 113Combined sources5
Beta strandi117 – 119Combined sources3
Beta strandi122 – 124Combined sources3
Helixi126 – 136Combined sources11
Beta strandi144 – 147Combined sources4
Turni150 – 152Combined sources3
Helixi153 – 155Combined sources3
Beta strandi156 – 158Combined sources3
Beta strandi161 – 170Combined sources10
Beta strandi173 – 184Combined sources12
Turni185 – 188Combined sources4
Helixi189 – 207Combined sources19
Beta strandi210 – 224Combined sources15
Helixi225 – 227Combined sources3
Helixi228 – 236Combined sources9
Beta strandi244 – 247Combined sources4
Helixi254 – 256Combined sources3
Helixi259 – 261Combined sources3
Beta strandi262 – 266Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B02X-ray2.50A1-279[»]
1BKOX-ray2.75A/B/C/D2-279[»]
1BKPX-ray1.70A/B2-279[»]
1BSFX-ray2.20A/B2-279[»]
1BSPX-ray2.50A/B2-279[»]
ProteinModelPortaliP0CI79.
SMRiP0CI79.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CI79.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0V. Bacteria.
COG0207. LUCA.
HOGENOMiHOG000257898.
InParanoidiP0CI79.
KOiK00560.
OMAiFEAPELW.
PhylomeDBiP0CI79.

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact. 1 hit.
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. 1 hit.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CI79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQFDKQYNS IIKDIINNGI SDEEFDVRTK WDSDGTPAHT LSVISKQMRF
60 70 80 90 100
DNSEVPILTT KKVAWKTAIK ELLWIWQLKS NDVNDLNMMG VHIWDQWKQE
110 120 130 140 150
DGTIGHAYGF QLGKKNRSLN GEKVDQVDYL LHQLKNNPSS RRHITMLWNP
160 170 180 190 200
DELDAMALTP CVYETQWYVK HGKLHLEVRA RSNDMALGNP FNVFQYNVLQ
210 220 230 240 250
RMIAQVTGYE LGEYIFNIGD CHVYTRHIDN LKIQMEREQF EAPELWINPE
260 270
VKDFYDFTID DFKLINYKHG DKLLFEVAV
Length:279
Mass (Da):32,807
Last modified:January 11, 2011 - v1
Checksum:iCC0B127AAF7912BD
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti84 – 85ND → TE in strain: ATCC 6633. 2
Natural varianti88M → K in strain: ATCC 6633. 1
Natural varianti118S → N in strain: ATCC 6633. 1
Natural varianti155A → S in strain: ATCC 6633. 1
Natural varianti171H → Q in strain: ATCC 6633. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78560 Genomic DNA. Translation: CAA55307.1.
AL009126 Genomic DNA. Translation: CAB13652.1.
AF004102 Genomic DNA. Translation: AAC26324.1.
PIRiI40494.
RefSeqiNP_389651.1. NC_000964.3.
WP_003244896.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13652; CAB13652; BSU17680.
GeneIDi939555.
KEGGibsu:BSU17680.
PATRICi18975359. VBIBacSub10457_1871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78560 Genomic DNA. Translation: CAA55307.1.
AL009126 Genomic DNA. Translation: CAB13652.1.
AF004102 Genomic DNA. Translation: AAC26324.1.
PIRiI40494.
RefSeqiNP_389651.1. NC_000964.3.
WP_003244896.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B02X-ray2.50A1-279[»]
1BKOX-ray2.75A/B/C/D2-279[»]
1BKPX-ray1.70A/B2-279[»]
1BSFX-ray2.20A/B2-279[»]
1BSPX-ray2.50A/B2-279[»]
ProteinModelPortaliP0CI79.
SMRiP0CI79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009726.

Proteomic databases

PaxDbiP0CI79.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13652; CAB13652; BSU17680.
GeneIDi939555.
KEGGibsu:BSU17680.
PATRICi18975359. VBIBacSub10457_1871.

Phylogenomic databases

eggNOGiENOG4105C0V. Bacteria.
COG0207. LUCA.
HOGENOMiHOG000257898.
InParanoidiP0CI79.
KOiK00560.
OMAiFEAPELW.
PhylomeDBiP0CI79.

Enzyme and pathway databases

UniPathwayiUPA00575.
BRENDAi2.1.1.45. 658.
SABIO-RKP0CI79.

Miscellaneous databases

EvolutionaryTraceiP0CI79.

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact. 1 hit.
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. 1 hit.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTYSY1_BACSU
AccessioniPrimary (citable) accession number: P0CI79
Secondary accession number(s): O30395, O30396, P42326
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 44 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.