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P0A884

- TYSY_ECOLI

UniProt

P0A884 - TYSY_ECOLI

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Protein
Thymidylate synthase
Gene
thyA, b2827, JW2795
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Provides the sole de novo source of dTMP for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

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

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. thymidylate synthase activity Source: EcoCyc

GO - Biological processi

  1. dTMP biosynthetic process Source: UniProtKB-HAMAP
  2. dTTP biosynthetic process Source: UniProtKB-UniPathway
  3. regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Nucleotide biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:THYMIDYLATESYN-MONOMER.
ECOL316407:JW2795-MONOMER.
MetaCyc:THYMIDYLATESYN-MONOMER.
SABIO-RKP0A884.
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:b2827, JW2795
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11002. thyA.

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 synthaseUniRule annotation
PRO_0000140954Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Although not discussed in the published references, Met-1 is represented in the submitted PDB entries as being modified by either a formyl, or a carboxyl group. The N-terminal is probably N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine.UniRule annotation

Keywords - PTMi

Formylation

Proteomic databases

PaxDbiP0A884.
PRIDEiP0A884.

Expressioni

Gene expression databases

GenevestigatoriP0A884.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-48261N.
IntActiP0A884. 5 interactions.
MINTiMINT-1265510.
STRINGi511145.b2827.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1413
Beta strandi16 – 183
Beta strandi21 – 233
Beta strandi26 – 3712
Helixi38 – 403
Beta strandi46 – 483
Helixi52 – 6413
Helixi70 – 745
Helixi81 – 833
Helixi94 – 1007
Beta strandi101 – 1033
Turni104 – 1063
Beta strandi107 – 1093
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
Helixi239 – 2413
Helixi244 – 2463
Beta strandi247 – 2515

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIQX-ray2.20A/B1-264[»]
1AJMX-ray2.40A1-264[»]
1AN5X-ray2.60A/B1-264[»]
1AOBX-ray2.10A1-264[»]
1AXWX-ray1.70A/B1-264[»]
1BDUX-ray2.10A1-264[»]
1BIDX-ray2.20A1-264[»]
1BJGX-ray2.30A1-264[»]
1BQ1X-ray2.50A/B1-264[»]
1BQ2X-ray2.20A1-264[»]
1DDUX-ray2.10A/B1-264[»]
1DNAX-ray2.20A/B1-264[»]
1EV5X-ray1.70A1-264[»]
1EV8X-ray2.60A1-264[»]
1EVFX-ray1.70A1-264[»]
1EVGX-ray2.00A1-264[»]
1F4BX-ray1.75A1-264[»]
1F4CX-ray2.00A/B1-264[»]
1F4DX-ray2.15A/B1-264[»]
1F4EX-ray1.90A1-264[»]
1F4FX-ray2.00A/B1-264[»]
1F4GX-ray1.75A/B1-264[»]
1FFLX-ray2.94A1-264[»]
1FWMX-ray2.20A/B1-264[»]
1JG0X-ray2.00A/B1-264[»]
1JTQX-ray2.50A/B1-264[»]
1JTUX-ray2.20A/B1-264[»]
1JUTX-ray2.70A/B1-264[»]
1KCEX-ray2.00A/B1-264[»]
1KZIX-ray1.75A/B1-264[»]
1KZJX-ray2.60A/B/C/D/E/F1-264[»]
1NCEX-ray2.40A/B1-264[»]
1QQQX-ray1.50A1-264[»]
1SYNX-ray2.00A/B1-264[»]
1TDUX-ray2.10A/B1-264[»]
1TJSX-ray2.20A1-264[»]
1TLCX-ray2.10A/B1-264[»]
1TLSX-ray2.60A/B1-264[»]
1TRGX-ray1.90A1-264[»]
1TSDX-ray1.95A/B1-264[»]
1TSNX-ray2.20A1-264[»]
1TYSX-ray1.80A1-264[»]
1ZPRX-ray2.50A/B1-264[»]
2A9WX-ray1.65A/B/C/D1-264[»]
2BBQX-ray2.30A/B1-264[»]
2FTNX-ray1.60A1-264[»]
2FTOX-ray2.00X1-264[»]
2FTQX-ray1.81A1-264[»]
2G8XX-ray1.83A/B1-264[»]
2KCEX-ray2.20A/B1-264[»]
2TSCX-ray1.97A/B1-264[»]
2VETX-ray2.20A1-264[»]
2VF0X-ray3.00A/B1-264[»]
3B5BX-ray2.70A/B1-264[»]
3B9HX-ray2.49A1-264[»]
3BFIX-ray2.20A1-264[»]
3BGXX-ray1.93A1-264[»]
3BHLX-ray1.40A/B1-264[»]
3BHRX-ray1.90A1-264[»]
3TMSX-ray2.10A1-264[»]
4F2VX-ray2.49A/B1-264[»]
4GEVX-ray1.30A/B1-264[»]
4ISKX-ray1.75A/B/C/D/E/F/G/H2-264[»]
4KNZX-ray1.30A/B1-264[»]
ProteinModelPortaliP0A884.
SMRiP0A884. Positions 2-264.

Miscellaneous databases

EvolutionaryTraceiP0A884.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0207.
HOGENOMiHOG000257900.
KOiK00560.
OMAiDVHLYSN.
OrthoDBiEOG6K6V53.
PhylomeDBiP0A884.

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.

P0A884-1 [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
J01710 Genomic DNA. Translation: AAA24675.1.
U29581 Genomic DNA. Translation: AAB40474.1.
U00096 Genomic DNA. Translation: AAC75866.1.
AP009048 Genomic DNA. Translation: BAE76896.1.
X03966 Genomic DNA. Translation: CAA27600.1.
PIRiA00549. SYECT.
RefSeqiNP_417304.1. NC_000913.3.
YP_491032.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75866; AAC75866; b2827.
BAE76896; BAE76896; BAE76896.
GeneIDi12933064.
949035.
KEGGiecj:Y75_p2761.
eco:b2827.
PATRICi32121072. VBIEscCol129921_2925.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01710 Genomic DNA. Translation: AAA24675.1 .
U29581 Genomic DNA. Translation: AAB40474.1 .
U00096 Genomic DNA. Translation: AAC75866.1 .
AP009048 Genomic DNA. Translation: BAE76896.1 .
X03966 Genomic DNA. Translation: CAA27600.1 .
PIRi A00549. SYECT.
RefSeqi NP_417304.1. NC_000913.3.
YP_491032.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AIQ X-ray 2.20 A/B 1-264 [» ]
1AJM X-ray 2.40 A 1-264 [» ]
1AN5 X-ray 2.60 A/B 1-264 [» ]
1AOB X-ray 2.10 A 1-264 [» ]
1AXW X-ray 1.70 A/B 1-264 [» ]
1BDU X-ray 2.10 A 1-264 [» ]
1BID X-ray 2.20 A 1-264 [» ]
1BJG X-ray 2.30 A 1-264 [» ]
1BQ1 X-ray 2.50 A/B 1-264 [» ]
1BQ2 X-ray 2.20 A 1-264 [» ]
1DDU X-ray 2.10 A/B 1-264 [» ]
1DNA X-ray 2.20 A/B 1-264 [» ]
1EV5 X-ray 1.70 A 1-264 [» ]
1EV8 X-ray 2.60 A 1-264 [» ]
1EVF X-ray 1.70 A 1-264 [» ]
1EVG X-ray 2.00 A 1-264 [» ]
1F4B X-ray 1.75 A 1-264 [» ]
1F4C X-ray 2.00 A/B 1-264 [» ]
1F4D X-ray 2.15 A/B 1-264 [» ]
1F4E X-ray 1.90 A 1-264 [» ]
1F4F X-ray 2.00 A/B 1-264 [» ]
1F4G X-ray 1.75 A/B 1-264 [» ]
1FFL X-ray 2.94 A 1-264 [» ]
1FWM X-ray 2.20 A/B 1-264 [» ]
1JG0 X-ray 2.00 A/B 1-264 [» ]
1JTQ X-ray 2.50 A/B 1-264 [» ]
1JTU X-ray 2.20 A/B 1-264 [» ]
1JUT X-ray 2.70 A/B 1-264 [» ]
1KCE X-ray 2.00 A/B 1-264 [» ]
1KZI X-ray 1.75 A/B 1-264 [» ]
1KZJ X-ray 2.60 A/B/C/D/E/F 1-264 [» ]
1NCE X-ray 2.40 A/B 1-264 [» ]
1QQQ X-ray 1.50 A 1-264 [» ]
1SYN X-ray 2.00 A/B 1-264 [» ]
1TDU X-ray 2.10 A/B 1-264 [» ]
1TJS X-ray 2.20 A 1-264 [» ]
1TLC X-ray 2.10 A/B 1-264 [» ]
1TLS X-ray 2.60 A/B 1-264 [» ]
1TRG X-ray 1.90 A 1-264 [» ]
1TSD X-ray 1.95 A/B 1-264 [» ]
1TSN X-ray 2.20 A 1-264 [» ]
1TYS X-ray 1.80 A 1-264 [» ]
1ZPR X-ray 2.50 A/B 1-264 [» ]
2A9W X-ray 1.65 A/B/C/D 1-264 [» ]
2BBQ X-ray 2.30 A/B 1-264 [» ]
2FTN X-ray 1.60 A 1-264 [» ]
2FTO X-ray 2.00 X 1-264 [» ]
2FTQ X-ray 1.81 A 1-264 [» ]
2G8X X-ray 1.83 A/B 1-264 [» ]
2KCE X-ray 2.20 A/B 1-264 [» ]
2TSC X-ray 1.97 A/B 1-264 [» ]
2VET X-ray 2.20 A 1-264 [» ]
2VF0 X-ray 3.00 A/B 1-264 [» ]
3B5B X-ray 2.70 A/B 1-264 [» ]
3B9H X-ray 2.49 A 1-264 [» ]
3BFI X-ray 2.20 A 1-264 [» ]
3BGX X-ray 1.93 A 1-264 [» ]
3BHL X-ray 1.40 A/B 1-264 [» ]
3BHR X-ray 1.90 A 1-264 [» ]
3TMS X-ray 2.10 A 1-264 [» ]
4F2V X-ray 2.49 A/B 1-264 [» ]
4GEV X-ray 1.30 A/B 1-264 [» ]
4ISK X-ray 1.75 A/B/C/D/E/F/G/H 2-264 [» ]
4KNZ X-ray 1.30 A/B 1-264 [» ]
ProteinModelPortali P0A884.
SMRi P0A884. Positions 2-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48261N.
IntActi P0A884. 5 interactions.
MINTi MINT-1265510.
STRINGi 511145.b2827.

Chemistry

BindingDBi P0A884.
ChEMBLi CHEMBL2555.

Proteomic databases

PaxDbi P0A884.
PRIDEi P0A884.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75866 ; AAC75866 ; b2827 .
BAE76896 ; BAE76896 ; BAE76896 .
GeneIDi 12933064.
949035.
KEGGi ecj:Y75_p2761.
eco:b2827.
PATRICi 32121072. VBIEscCol129921_2925.

Organism-specific databases

EchoBASEi EB0995.
EcoGenei EG11002. thyA.

Phylogenomic databases

eggNOGi COG0207.
HOGENOMi HOG000257900.
KOi K00560.
OMAi DVHLYSN.
OrthoDBi EOG6K6V53.
PhylomeDBi P0A884.

Enzyme and pathway databases

UniPathwayi UPA00575 .
BioCyci EcoCyc:THYMIDYLATESYN-MONOMER.
ECOL316407:JW2795-MONOMER.
MetaCyc:THYMIDYLATESYN-MONOMER.
SABIO-RK P0A884.

Miscellaneous databases

EvolutionaryTracei P0A884.
PROi P0A884.

Gene expression databases

Genevestigatori P0A884.

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

« Hide 'large scale' publications
  1. "Primary structure of the Escherichia coli thyA gene and its thymidylate synthase product."
    Belfort M., Maley G.F., Pedersen-Lane J., Maley F.
    Proc. Natl. Acad. Sci. U.S.A. 80:4914-4918(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12 / JM103 / ATCC 39403 / DSM 2829 / NCIMB 12044.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Complete nucleotide sequence of the Escherichia coli recC gene and of the thyA-recC intergenic region."
    Finch P.W., Wilson R.E., Brown K., Hickson I.D., Tomkinson A.E., Emmerson P.T.
    Nucleic Acids Res. 14:4437-4451(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-264.
  5. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  6. "Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate."
    Montfort W.R., Perry K.M., Fauman E.B., Finer-Moore J.S., Maley G.F., Hardy L., Maley F., Stroud R.M.
    Biochemistry 29:6964-6977(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS).
  7. "Characterization of a specific interaction between Escherichia coli thymidylate synthase and Escherichia coli thymidylate synthase mRNA."
    Voeller D.M., Changchien L.-M., Maley G.F., Maley F., Takechi T., Turner R.E., Montfort W.R., Allegra C.J., Chu E.
    Nucleic Acids Res. 23:869-875(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF TRANSLATION REGULATION.
  8. "Amino acid substitution analysis of E. coli thymidylate synthase: the study of a highly conserved region at the N-terminus."
    Kim C.W., Michaels M.L., Miller J.F.
    Proteins 13:352-363(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  9. "Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases."
    Perry K.M., Fauman E.B., Finer-Moore J.S., Montfort W.R., Maley G.F., Maley F., Stroud R.M.
    Proteins 8:315-333(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  10. "Water-mediated substrate/product discrimination: the product complex of thymidylate synthase at 1.83 A."
    Fauman E.B., Rutenber E.E., Maley G.F., Maley F., Stroud R.M.
    Biochemistry 33:1502-1511(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
  11. "An essential role for water in an enzyme reaction mechanism: the crystal structure of the thymidylate synthase mutant E58Q."
    Sage C.R., Rutenber E.E., Stout T.J., Stroud R.M.
    Biochemistry 35:16270-16281(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-58.
  12. "Crystal structures of a marginally active thymidylate synthase mutant, Arg 126-->Glu."
    Strop P., Changchien L., Maley F., Montfort W.R.
    Protein Sci. 6:2504-2511(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT GLU-126.
  13. "Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer."
    Reyes C.L., Sage C.R., Rutenber E.E., Nissen R.M., Finer-Moore J.S., Stroud R.M.
    J. Mol. Biol. 284:699-712(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ALA-177.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

Entry informationi

Entry nameiTYSY_ECOLI
AccessioniPrimary (citable) accession number: P0A884
Secondary accession number(s): P00470, Q2MA10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 90 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, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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