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P0A886

- TYSY_ECO57

UniProt

P0A886 - TYSY_ECO57

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Protein

Thymidylate synthase

Gene
thyA, Z4144, ECs3684
Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei146 – 1461 By similarity

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 synthase (EC:2.1.1.45)
Short name:
TS
Short name:
TSase
Gene namesi
Name:thyA
Ordered Locus Names:Z4144, ECs3684
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 synthaseUniRule annotationPRO_0000140955Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Formylation

Interactioni

Subunit structurei

Homodimer By similarity.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 – 1413
Beta strandi16 – 194
Beta strandi25 – 3713
Helixi38 – 403
Beta strandi46 – 483
Helixi53 – 6412
Helixi70 – 745
Turni79 – 835
Helixi94 – 1007
Helixi111 – 12111
Beta strandi129 – 1313
Helixi135 – 1406
Beta strandi141 – 1433
Beta strandi146 – 15510
Beta strandi158 – 16912
Turni170 – 1734
Helixi174 – 19118
Beta strandi195 – 20915
Helixi210 – 2123
Helixi213 – 2208
Beta strandi229 – 2324
Helixi244 – 2463
Beta strandi247 – 2515

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LRRX-ray2.41A1-264[»]
ProteinModelPortaliP0A886.
SMRiP0A886. Positions 2-264.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0207.
HOGENOMiHOG000257900.
KOiK00560.
OMAiDVHLYSN.
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

MKQYLELMQK VLDEGTQKND RTGTGTLSIF GHQMRFNLQD GFPLVTTKRC    50
HLRSIIHELL WFLQGDTNIA YLHENNVTIW DEWADENGDL GPVYGKQWRA 100
WPTPDGRHID QITTVLNQLK NDPDSRRIIV SAWNVGELDK MALAPCHAFF 150
QFYVADGKLS CQLYQRSCDV FLGLPFNIAS YALLVHMMAQ QCDLEVGDFV 200
WTGGDTHLYS NHMDQTHLQL SREPRPLPKL IIKRKPESIF DYRFEDFEIE 250
GYDPHPGIKA PVAI 264
Length:264
Mass (Da):30,480
Last modified:July 21, 1986 - v1
Checksum:i0E6D88ED98D24D22
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG57938.1 .
BA000007 Genomic DNA. Translation: BAB37107.1 .
PIRi D91089.
F85934.
RefSeqi NP_289379.1. NC_002655.2.
NP_311711.1. NC_002695.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LRR X-ray 2.41 A 1-264 [» ]
ProteinModelPortali P0A886.
SMRi P0A886. Positions 2-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z4144.

Chemistry

BindingDBi P0A886.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG57938 ; AAG57938 ; Z4144 .
BAB37107 ; BAB37107 ; BAB37107 .
GeneIDi 916501.
959426.
KEGGi ece:Z4144.
ecs:ECs3684.
PATRICi 18356857. VBIEscCol44059_3608.

Phylogenomic databases

eggNOGi COG0207.
HOGENOMi HOG000257900.
KOi K00560.
OMAi DVHLYSN.
OrthoDBi EOG6K6V53.

Enzyme and pathway databases

UniPathwayi UPA00575 .
BioCyci ECOL386585:GJFA-3652-MONOMER.
ECOO157:THYA-MONOMER.
SABIO-RK P0A886.

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. 2 hits.
PROSITEi PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2001) [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 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 70 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

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