P13100 (TYSY_PNECA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thymidylate synthase
Short name=TS
Short name=TSase
EC=2.1.1.45

Gene names

Name:

THYA

Organism

Pneumocystis carinii

Taxonomic identifier

4754 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Pneumocystidomycetes › Pneumocystidales › Pneumocystidaceae › Pneumocystis

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
Pathway	Pyrimidine metabolism; dTTP biosynthesis.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the thymidylate synthase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Molecular function	Methyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	dTMP biosynthetic process Inferred from electronic annotation. Source: InterPro dTTP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	thymidylate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 297

297

Thymidylate synthase

PRO_0000140911

Sites

Active site

173

1

Secondary structure

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297

Helix Strand Turn

Details...

Helix

4 – 19

16

Beta strand

21 – 24

4

Beta strand

28 – 36

9

Beta strand

40 – 43

4

Helix

45 – 47

3

Beta strand

53 – 55

3

Helix

59 – 70

12

Helix

76 – 80

5

Turn

81 – 83

3

Helix

88 – 91

4

Helix

93 – 98

6

Helix

113 – 119

7

Helix

138 – 148

11

Beta strand

156 – 158

3

Turn

162 – 164

3

Helix

165 – 167

3

Beta strand

168 – 170

3

Beta strand

173 – 181

9

Beta strand

191 – 202

12

Turn

203 – 205

3

Helix

206 – 224

19

Beta strand

228 – 242

15

Helix

243 – 250

8

Helix

252 – 254

3

Beta strand

262 – 265

4

Helix

272 – 274

3

Helix

277 – 279

3

Beta strand

280 – 284

5

Sequences

	Sequence		Length	Mass (Da)
	P13100 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 985F6F870EF2A7B2	FASTA	297	34,362
	10 20 30 40 50 60 MVNAEEQQYL NLVQYIINHG EDRPDRTGTG TLSVFAPSPL KFSLRNKTFP LLTTKRVFIR 70 80 90 100 110 120 GVIEELLWFI RGETDSLKLR EKNIHIWDAN GSREYLDSIG LTKRQEGDLG PIYGFQWRHF 130 140 150 160 170 180 GAEYIDCKTN YIGQGVDQLA NIIQKIRTSP YDRRLILSAW NPADLEKMAL PPCHMFCQFY 190 200 210 220 230 240 VHIPSNNHRP ELSCQLYQRS CDMGLGVPFN IASYALLTCM IAHVCDLDPG DFIHVMGDCH 250 260 270 280 290 IYKDHIEALQ QQLTRSPRPF PTLSLNRSIT DIEDFTLDDF NIQNYHPYET IKMKMSI

References

[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M25415 Genomic DNA. Translation: AAA33802.1.
S77510 Genomic DNA. Translation: AAB34157.1.

PIR

YXUNTP. A33720.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P13100.

SMR

P13100. Positions 3-297.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00575.

Family and domain databases

Gene3D

3.30.572.10. 1 hit.

InterPro

IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]

Pfam

PF00303. Thymidylat_synt. 1 hit.
[Graphical view]

PRINTS

PR00108. THYMDSNTHASE.

SUPFAM

SSF55831. Thymidylat_synth_C. 1 hit.

TIGRFAMs

TIGR03284. thym_sym. 1 hit.

PROSITE

PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P13100.

EvolutionaryTrace

P13100.

Entry information

Entry name

TYSY_PNECA

Accession

Primary (citable) accession number: P13100

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program