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Protein

Thymidylate synthase

Gene

THYA

Organism
Pneumocystis carinii
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: dTTP biosynthesis

This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.
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 sitei26dUMPBy similarity1
Active sitei173NucleophileBy similarity1
Binding sitei2025,10-methylenetetrahydrofolateBy similarity1
Binding sitei210dUMPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi153 – 154dUMP; shared with dimeric partnerBy similarity2
Nucleotide bindingi199 – 202dUMPBy similarity4
Nucleotide bindingi240 – 242dUMPBy similarity3

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. 4924.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthase (EC:2.1.1.45)
Short name:
TS
Short name:
TSase
Gene namesi
Name:THYA
OrganismiPneumocystis carinii
Taxonomic identifieri4754 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3085612.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001409111 – 297Thymidylate synthaseAdd BLAST297

Interactioni

Subunit structurei

Homodimer.

Chemistry databases

BindingDBiP13100.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 19Combined sources16
Beta strandi21 – 24Combined sources4
Beta strandi28 – 36Combined sources9
Beta strandi40 – 43Combined sources4
Helixi45 – 47Combined sources3
Beta strandi53 – 55Combined sources3
Helixi59 – 70Combined sources12
Helixi76 – 80Combined sources5
Turni81 – 83Combined sources3
Helixi88 – 91Combined sources4
Helixi93 – 98Combined sources6
Helixi113 – 119Combined sources7
Helixi138 – 148Combined sources11
Beta strandi156 – 158Combined sources3
Turni162 – 164Combined sources3
Helixi165 – 167Combined sources3
Beta strandi168 – 170Combined sources3
Beta strandi173 – 181Combined sources9
Beta strandi191 – 202Combined sources12
Turni203 – 205Combined sources3
Helixi206 – 224Combined sources19
Beta strandi228 – 242Combined sources15
Helixi243 – 250Combined sources8
Helixi252 – 254Combined sources3
Beta strandi262 – 265Combined sources4
Helixi272 – 274Combined sources3
Helixi277 – 279Combined sources3
Beta strandi280 – 284Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CI7X-ray2.60A/B1-297[»]
1F28X-ray1.90A/B/C/D1-297[»]
ProteinModelPortaliP13100.
SMRiP13100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13100.

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidylate synthase family.Curated

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.

P13100-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNAEEQQYL NLVQYIINHG EDRPDRTGTG TLSVFAPSPL KFSLRNKTFP
60 70 80 90 100
LLTTKRVFIR GVIEELLWFI RGETDSLKLR EKNIHIWDAN GSREYLDSIG
110 120 130 140 150
LTKRQEGDLG PIYGFQWRHF GAEYIDCKTN YIGQGVDQLA NIIQKIRTSP
160 170 180 190 200
YDRRLILSAW NPADLEKMAL PPCHMFCQFY VHIPSNNHRP ELSCQLYQRS
210 220 230 240 250
CDMGLGVPFN IASYALLTCM IAHVCDLDPG DFIHVMGDCH IYKDHIEALQ
260 270 280 290
QQLTRSPRPF PTLSLNRSIT DIEDFTLDDF NIQNYHPYET IKMKMSI
Length:297
Mass (Da):34,362
Last modified:January 1, 1990 - v1
Checksum:i985F6F870EF2A7B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25415 Genomic DNA. Translation: AAA33802.1.
S77510 Genomic DNA. Translation: AAB34157.1.
PIRiA33720. YXUNTP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25415 Genomic DNA. Translation: AAA33802.1.
S77510 Genomic DNA. Translation: AAB34157.1.
PIRiA33720. YXUNTP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CI7X-ray2.60A/B1-297[»]
1F28X-ray1.90A/B/C/D1-297[»]
ProteinModelPortaliP13100.
SMRiP13100.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP13100.
ChEMBLiCHEMBL3085612.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00575.
BRENDAi2.1.1.45. 4924.

Miscellaneous databases

EvolutionaryTraceiP13100.

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 nameiTYSY_PNECA
AccessioniPrimary (citable) accession number: P13100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.