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P13100

- TYSY_PNECA

UniProt

P13100 - TYSY_PNECA

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Protein

Thymidylate synthase

Gene

THYA

Organism
Pneumocystis carinii
Status
Reviewed - 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

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 – 1916
Beta strandi21 – 244
Beta strandi28 – 369
Beta strandi40 – 434
Helixi45 – 473
Beta strandi53 – 553
Helixi59 – 7012
Helixi76 – 805
Turni81 – 833
Helixi88 – 914
Helixi93 – 986
Helixi113 – 1197
Helixi138 – 14811
Beta strandi156 – 1583
Turni162 – 1643
Helixi165 – 1673
Beta strandi168 – 1703
Beta strandi173 – 1819
Beta strandi191 – 20212
Turni203 – 2053
Helixi206 – 22419
Beta strandi228 – 24215
Helixi243 – 2508
Helixi252 – 2543
Beta strandi262 – 2654
Helixi272 – 2743
Helixi277 – 2793
Beta strandi280 – 2845

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI7X-ray2.60A/B1-297[»]
1F28X-ray1.90A/B/C/D1-297[»]
ProteinModelPortaliP13100.
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:
EMBL
GenBank
DDBJ
Links Updated
M25415 Genomic DNA. Translation: AAA33802.1.
S77510 Genomic DNA. Translation: AAB34157.1.
PIRiA33720. YXUNTP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M25415 Genomic DNA. Translation: AAA33802.1 .
S77510 Genomic DNA. Translation: AAB34157.1 .
PIRi A33720. YXUNTP.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CI7 X-ray 2.60 A/B 1-297 [» ]
1F28 X-ray 1.90 A/B/C/D 1-297 [» ]
ProteinModelPortali P13100.
SMRi P13100. Positions 3-297.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P13100.
ChEMBLi CHEMBL3085612.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00575 .

Miscellaneous databases

EvolutionaryTracei P13100.

Family and domain databases

Gene3Di 3.30.572.10. 1 hit.
HAMAPi MF_00008. Thymidy_synth_bact.
InterProi IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view ]
Pfami PF00303. Thymidylat_synt. 1 hit.
[Graphical view ]
PRINTSi PR00108. THYMDSNTHASE.
SUPFAMi SSF55831. SSF55831. 1 hit.
TIGRFAMsi TIGR03284. thym_sym. 1 hit.
PROSITEi PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1989) [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(1995) [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(1999) [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: October 29, 2014
This is version 86 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