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Protein

Thymidylate synthase

Gene

thyA

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Provides the sole de novo source of dTMP for DNA biosynthesis.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei146 – 1461UniRule annotation

GO - Molecular functioni

  1. thymidylate synthase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. dTMP biosynthetic process Source: UniProtKB-HAMAP
  2. dTTP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3652-MONOMER.
ECOO157:THYA-MONOMER.
SABIO-RKP0A886.
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
Ordered Locus Names:Z4144, ECs3684
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558 Componenti: Chromosome UP000002519 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Thymidylate synthasePRO_0000140955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionineBy similarity

Post-translational modificationi

The N-terminal is probably N-(dihydroxymethyl)-methionine, the hydrated form of N-formylmethionine.By similarity

Keywords - PTMi

Formylation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z4144.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1413Combined sources
Beta strandi16 – 194Combined sources
Beta strandi25 – 3713Combined sources
Helixi38 – 403Combined sources
Beta strandi46 – 483Combined sources
Helixi53 – 6412Combined sources
Helixi70 – 745Combined sources
Turni79 – 835Combined sources
Helixi94 – 1007Combined sources
Helixi111 – 12111Combined sources
Beta strandi129 – 1313Combined sources
Helixi135 – 1406Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi146 – 15510Combined sources
Beta strandi158 – 16912Combined sources
Turni170 – 1734Combined sources
Helixi174 – 19118Combined sources
Beta strandi195 – 20915Combined sources
Helixi210 – 2123Combined sources
Helixi213 – 2208Combined sources
Beta strandi229 – 2324Combined sources
Helixi244 – 2463Combined sources
Beta strandi247 – 2515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LRRX-ray2.41A1-264[»]
ProteinModelPortaliP0A886.
SMRiP0A886. Positions 2-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0207.
HOGENOMiHOG000257900.
KOiK00560.
OMAiNEWADEN.
OrthoDBiEOG6K6V53.

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. 2 hits.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A886-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQYLELMQK VLDEGTQKND RTGTGTLSIF GHQMRFNLQD GFPLVTTKRC
60 70 80 90 100
HLRSIIHELL WFLQGDTNIA YLHENNVTIW DEWADENGDL GPVYGKQWRA
110 120 130 140 150
WPTPDGRHID QITTVLNQLK NDPDSRRIIV SAWNVGELDK MALAPCHAFF
160 170 180 190 200
QFYVADGKLS CQLYQRSCDV FLGLPFNIAS YALLVHMMAQ QCDLEVGDFV
210 220 230 240 250
WTGGDTHLYS NHMDQTHLQL SREPRPLPKL IIKRKPESIF DYRFEDFEIE
260
GYDPHPGIKA PVAI
Length:264
Mass (Da):30,480
Last modified:July 20, 1986 - v1
Checksum:i0E6D88ED98D24D22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57938.1.
BA000007 Genomic DNA. Translation: BAB37107.1.
PIRiD91089.
F85934.
RefSeqiNP_289379.1. NC_002655.2.
NP_311711.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG57938; AAG57938; Z4144.
BAB37107; BAB37107; BAB37107.
GeneIDi916501.
959426.
KEGGiece:Z4144.
ecs:ECs3684.
PATRICi18356857. VBIEscCol44059_3608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57938.1.
BA000007 Genomic DNA. Translation: BAB37107.1.
PIRiD91089.
F85934.
RefSeqiNP_289379.1. NC_002655.2.
NP_311711.1. NC_002695.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LRRX-ray2.41A1-264[»]
ProteinModelPortaliP0A886.
SMRiP0A886. Positions 2-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z4144.

Chemistry

BindingDBiP0A886.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57938; AAG57938; Z4144.
BAB37107; BAB37107; BAB37107.
GeneIDi916501.
959426.
KEGGiece:Z4144.
ecs:ECs3684.
PATRICi18356857. VBIEscCol44059_3608.

Phylogenomic databases

eggNOGiCOG0207.
HOGENOMiHOG000257900.
KOiK00560.
OMAiNEWADEN.
OrthoDBiEOG6K6V53.

Enzyme and pathway databases

UniPathwayiUPA00575.
BioCyciECOL386585:GJFA-3652-MONOMER.
ECOO157:THYA-MONOMER.
SABIO-RKP0A886.

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

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiTYSY_ECO57
AccessioniPrimary (citable) accession number: P0A886
Secondary accession number(s): P00470
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: July 20, 1986
Last modified: January 6, 2015
This is version 74 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, Complete proteome

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.