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Protein

Thymidylate synthase

Gene

thyA

Organism
Lactobacillus casei
Status
Reviewed-Annotation score: Annotation score: 3 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

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
Binding sitei23dUMPUniRule annotation1
Active sitei198NucleophileUniRule annotation1
Binding sitei2215,10-methylenetetrahydrofolateUniRule annotation1
Binding sitei229dUMPUniRule annotation1
Binding sitei3155,10-methylenetetrahydrofolate; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi178 – 179dUMP; shared with dimeric partnerUniRule annotation2
Nucleotide bindingi218 – 221dUMPUniRule annotation4
Nucleotide bindingi259 – 261dUMPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

SABIO-RKP00469.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthaseUniRule annotation (EC:2.1.1.45UniRule annotation)
Short name:
TSUniRule annotation
Short name:
TSaseUniRule annotation
Gene namesi
Name:thyAUniRule annotation
OrganismiLactobacillus casei
Taxonomic identifieri1582 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5328.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001409671 – 316Thymidylate synthaseAdd BLAST316

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Chemistry databases

BindingDBiP00469.

Structurei

Secondary structure

1316
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 16Combined sources13
Beta strandi18 – 22Combined sources5
Turni23 – 25Combined sources3
Beta strandi26 – 33Combined sources8
Beta strandi35 – 39Combined sources5
Helixi40 – 42Combined sources3
Beta strandi48 – 50Combined sources3
Helixi54 – 65Combined sources12
Helixi71 – 75Combined sources5
Turni76 – 78Combined sources3
Helixi83 – 90Combined sources8
Beta strandi93 – 95Combined sources3
Beta strandi98 – 100Combined sources3
Helixi101 – 103Combined sources3
Helixi104 – 110Combined sources7
Helixi112 – 131Combined sources20
Helixi133 – 139Combined sources7
Beta strandi143 – 145Combined sources3
Helixi146 – 151Combined sources6
Beta strandi152 – 154Combined sources3
Beta strandi156 – 158Combined sources3
Helixi163 – 173Combined sources11
Beta strandi174 – 176Combined sources3
Beta strandi181 – 183Combined sources3
Turni187 – 192Combined sources6
Beta strandi193 – 195Combined sources3
Beta strandi198 – 207Combined sources10
Beta strandi210 – 221Combined sources12
Turni222 – 224Combined sources3
Helixi225 – 244Combined sources20
Beta strandi247 – 261Combined sources15
Helixi262 – 264Combined sources3
Helixi265 – 271Combined sources7
Beta strandi281 – 284Combined sources4
Helixi291 – 293Combined sources3
Helixi296 – 298Combined sources3
Beta strandi299 – 302Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BO7X-ray2.40A1-316[»]
1BO8X-ray2.40A1-316[»]
1BP0X-ray2.40A1-316[»]
1BP6X-ray2.40A1-316[»]
1BPJX-ray2.40A1-316[»]
1JMFX-ray2.50A1-316[»]
1JMGX-ray2.20A1-316[»]
1JMHX-ray2.50A1-316[»]
1JMIX-ray2.50A1-316[»]
1LCAX-ray2.50A1-316[»]
1LCBX-ray2.50A1-316[»]
1LCEX-ray2.50A1-316[»]
1NJAX-ray2.50A1-316[»]
1NJBX-ray2.74A1-316[»]
1NJCX-ray2.50A1-316[»]
1NJDX-ray2.20A1-316[»]
1NJEX-ray2.30A1-316[»]
1TDAX-ray3.09A1-315[»]
1TDBX-ray2.65A1-315[»]
1TDCX-ray2.65A1-315[»]
1THYX-ray2.90A1-316[»]
1TSLX-ray2.50A1-316[»]
1TSMX-ray3.00A1-316[»]
1TSVX-ray2.90A1-316[»]
1TSWX-ray2.50A1-316[»]
1TSXX-ray2.50A1-316[»]
1TSYX-ray2.20A1-316[»]
1TSZX-ray2.75A1-316[»]
1TVUX-ray2.50A1-316[»]
1TVVX-ray2.30A1-316[»]
1TVWX-ray2.50A1-316[»]
1VZAX-ray2.50A1-316[»]
1VZBX-ray2.50A1-316[»]
1VZCX-ray2.50A1-316[»]
1VZDX-ray2.50A1-316[»]
1VZEX-ray2.30A1-316[»]
2G86X-ray2.40A1-316[»]
2G89X-ray2.50A1-316[»]
2G8AX-ray2.40A1-316[»]
2G8DX-ray2.40A1-316[»]
2TDDX-ray2.70A1-315[»]
2TDMX-ray2.55A1-316[»]
3BNZX-ray2.60A1-316[»]
3BYXX-ray2.40A1-316[»]
3BZ0X-ray2.70A1-316[»]
3C06X-ray2.60A1-316[»]
3C0AX-ray2.40A1-316[»]
3IJZX-ray2.21A1-316[»]
3IK0X-ray2.10A1-316[»]
3IK1X-ray2.25A1-316[»]
4TMSX-ray2.35A1-316[»]
ProteinModelPortaliP00469.
SMRiP00469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00469.

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 2 hits.
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.

P00469-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEQPYLDLA KKVLDEGHFK PDRTHTGTYS IFGHQMRFDL SKGFPLLTTK
60 70 80 90 100
KVPFGLIKSE LLWFLHGDTN IRFLLQHRNH IWDEWAFEKW VKSDEYHGPD
110 120 130 140 150
MTDFGHRSQK DPEFAAVYHE EMAKFDDRVL HDDAFAAKYG DLGLVYGSQW
160 170 180 190 200
RAWHTSKGDT IDQLGDVIEQ IKTHPYSRRL IVSAWNPEDV PTMALPPCHT
210 220 230 240 250
LYQFYVNDGK LSLQLYQRSA DIFLGVPFNI ASYALLTHLV AHECGLEVGE
260 270 280 290 300
FIHTFGDAHL YVNHLDQIKE QLSRTPRPAP TLQLNPDKHD IFDFDMKDIK
310
LLNYDPYPAI KAPVAV
Length:316
Mass (Da):36,580
Last modified:July 21, 1986 - v1
Checksum:i4C391722044FF0A5
GO

Sequence cautioni

The sequence AAA25255 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19653 Genomic DNA. Translation: AAA25255.1. Different initiation.
PIRiA29817. SYLBT.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19653 Genomic DNA. Translation: AAA25255.1. Different initiation.
PIRiA29817. SYLBT.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BO7X-ray2.40A1-316[»]
1BO8X-ray2.40A1-316[»]
1BP0X-ray2.40A1-316[»]
1BP6X-ray2.40A1-316[»]
1BPJX-ray2.40A1-316[»]
1JMFX-ray2.50A1-316[»]
1JMGX-ray2.20A1-316[»]
1JMHX-ray2.50A1-316[»]
1JMIX-ray2.50A1-316[»]
1LCAX-ray2.50A1-316[»]
1LCBX-ray2.50A1-316[»]
1LCEX-ray2.50A1-316[»]
1NJAX-ray2.50A1-316[»]
1NJBX-ray2.74A1-316[»]
1NJCX-ray2.50A1-316[»]
1NJDX-ray2.20A1-316[»]
1NJEX-ray2.30A1-316[»]
1TDAX-ray3.09A1-315[»]
1TDBX-ray2.65A1-315[»]
1TDCX-ray2.65A1-315[»]
1THYX-ray2.90A1-316[»]
1TSLX-ray2.50A1-316[»]
1TSMX-ray3.00A1-316[»]
1TSVX-ray2.90A1-316[»]
1TSWX-ray2.50A1-316[»]
1TSXX-ray2.50A1-316[»]
1TSYX-ray2.20A1-316[»]
1TSZX-ray2.75A1-316[»]
1TVUX-ray2.50A1-316[»]
1TVVX-ray2.30A1-316[»]
1TVWX-ray2.50A1-316[»]
1VZAX-ray2.50A1-316[»]
1VZBX-ray2.50A1-316[»]
1VZCX-ray2.50A1-316[»]
1VZDX-ray2.50A1-316[»]
1VZEX-ray2.30A1-316[»]
2G86X-ray2.40A1-316[»]
2G89X-ray2.50A1-316[»]
2G8AX-ray2.40A1-316[»]
2G8DX-ray2.40A1-316[»]
2TDDX-ray2.70A1-315[»]
2TDMX-ray2.55A1-316[»]
3BNZX-ray2.60A1-316[»]
3BYXX-ray2.40A1-316[»]
3BZ0X-ray2.70A1-316[»]
3C06X-ray2.60A1-316[»]
3C0AX-ray2.40A1-316[»]
3IJZX-ray2.21A1-316[»]
3IK0X-ray2.10A1-316[»]
3IK1X-ray2.25A1-316[»]
4TMSX-ray2.35A1-316[»]
ProteinModelPortaliP00469.
SMRiP00469.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP00469.
ChEMBLiCHEMBL5328.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00575.
SABIO-RKP00469.

Miscellaneous databases

EvolutionaryTraceiP00469.

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 2 hits.
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 nameiTYSY_LACCA
AccessioniPrimary (citable) accession number: P00469
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.