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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei173 – 1731

GO - Molecular functioni

  1. thymidylate synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. dTMP biosynthetic process Source: InterPro
  2. dTTP biosynthetic process Source: UniProtKB-UniPathway
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Thymidylate synthasePRO_0000140911Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1916Combined sources
Beta strandi21 – 244Combined sources
Beta strandi28 – 369Combined sources
Beta strandi40 – 434Combined sources
Helixi45 – 473Combined sources
Beta strandi53 – 553Combined sources
Helixi59 – 7012Combined sources
Helixi76 – 805Combined sources
Turni81 – 833Combined sources
Helixi88 – 914Combined sources
Helixi93 – 986Combined sources
Helixi113 – 1197Combined sources
Helixi138 – 14811Combined sources
Beta strandi156 – 1583Combined sources
Turni162 – 1643Combined sources
Helixi165 – 1673Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi173 – 1819Combined sources
Beta strandi191 – 20212Combined sources
Turni203 – 2053Combined sources
Helixi206 – 22419Combined sources
Beta strandi228 – 24215Combined sources
Helixi243 – 2508Combined sources
Helixi252 – 2543Combined sources
Beta strandi262 – 2654Combined sources
Helixi272 – 2743Combined sources
Helixi277 – 2793Combined sources
Beta strandi280 – 2845Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI7X-ray2.60A/B1-297[»]
1F28X-ray1.90A/B/C/D1-297[»]
SMRiP13100. Positions 3-297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13100.

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidylate synthase family.Curated

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. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI7X-ray2.60A/B1-297[»]
1F28X-ray1.90A/B/C/D1-297[»]
SMRiP13100. Positions 3-297.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

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

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. 1 hit.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and expression of the Pneumocystis carinii thymidylate synthase gene."
    Edman U., Edman J.C., Lundgren B., Santi D.V.
    Proc. Natl. Acad. Sci. U.S.A. 86:6503-6507(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Polymorphism of the thymidylate synthase gene of Pneumocystis carinii from different host species."
    Mazars E., Odberg-Ferragut C., Dei-Cas E., Fourmaux M.N., Aliouat E.M., Brun-Pascaud M., Mougeot G., Camus D.
    J. Eukaryot. Microbiol. 42:26-32(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-210.
  3. "The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits."
    Anderson A.C., O'Neil R.H., DeLano W.L., Stroud R.M.
    Biochemistry 38:13829-13836(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

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: April 1, 2015
This is version 88 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

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.