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UniProtKB - P0A884 (TYSY_ECOLI)

Entry version 137 (02 Jun 2021)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
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Protein

Thymidylate synthase

Gene

thyA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product (PubMed:3286637, PubMed:2223754, PubMed:9826509).

This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation (PubMed:7708505).

4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 8.8 sec(-1).1 Publication
  1. KM=50 µM for dUMP1 Publication
  2. KM=25 µM for 5,10-methylenetetrahydrofolate1 Publication
  3. KM=4.1 µM for dUMP1 Publication
  4. KM=13.6 µM for 5,10-methylenetetrahydrofolate1 Publication
  1. Vmax=5.47 µmol/min/mg enzyme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: dTTP biosynthesis

This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway dTTP biosynthesis and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei21dUMPCombined sources2 Publications1
Binding sitei515,10-methylenetetrahydrofolateCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei146NucleophileUniRule annotation3 Publications1
Binding sitei1695,10-methylenetetrahydrofolateCombined sources1 Publication1
Binding sitei177dUMPCombined sources2 Publications1
Binding sitei2635,10-methylenetetrahydrofolate; via carbonyl oxygenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi126 – 127dUMP; shared with dimeric partnerCombined sources2 Publications2
Nucleotide bindingi166 – 169dUMPCombined sources2 Publications4
Nucleotide bindingi207 – 209dUMPCombined sources2 Publications3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMethyltransferase, Repressor, RNA-binding, Transferase
Biological processNucleotide biosynthesis, Translation regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:THYMIDYLATESYN-MONOMER
MetaCyc:THYMIDYLATESYN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.1.1.45, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0A884

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00575

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Thymidylate synthase3 PublicationsUniRule annotation (EC:2.1.1.45UniRule annotation3 Publications)
Short name:
TS3 PublicationsUniRule annotation
Short name:
TSaseUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:thyA1 PublicationUniRule annotation
Ordered Locus Names:b2827, JW2795
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi50C → Y: Shows 0.2% of wild-type catalytic activity, but substrate affinity is not affected. 1 Publication1
Mutagenesisi126R → E: Shows 2000-fold decrease in catalytic activity and 600-fold decrease in affinity for dUMP. 1 Publication1
Mutagenesisi177N → A: Shows 200-fold decrease in catalytic activity, 20-fold decrease in affinity for dUMP, and 10-fold decrease in affinity for mTHF. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2555

Drug and drug target database

More...DrugBanki		DB02031, (6S)-5,6,7,8-tetrahydrofolic acid
DB04447, 1,4-Dithiothreitol
DB03541, 10-Propargyl-5,8-Dideazafolic Acid
DB03274, 2',5'-Dideoxyuridine
DB04457, 2'-Deoxyguanosine-5'-Monophosphate
DB02256, 2'-Deoxyuridine
DB08131, 2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID
DB04696, 4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN
DB02301, 5,10-Methylene-6-Hydrofolic Acid
DB03761, 5-fluoro-2'-deoxyuridine-5'-monophosphate
DB03800, Deoxyuridine monophosphate
DB02467, L-methionine (S)-S-oxide
DB02223, LY231514 tetra glu
DB03038, LY341770
DB03157, N,O-Didansyl-L-Tyrosine
DB03818, N-[Tosyl-D-Prolinyl]Amino-Ethanethiol
DB02899, N-Carboxymethionine
DB04586, o-Bromophenol
DB04530, S,S-(2-Hydroxyethyl)Thiocysteine
DB04503, Sp-722
DB03558, SP-876
DB02752, Tosyl-D-Proline

DrugCentral

More...DrugCentrali		P0A884

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001409541 – 264Thymidylate synthaseAdd BLAST264

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.

Keywords - PTMi

Formylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A884

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P0A884

PRoteomics IDEntifications database

More...PRIDEi		P0A884

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4262058, 217 interactors

Database of interacting proteins

More...DIPi		DIP-48261N

Protein interaction database and analysis system

More...IntActi		P0A884, 5 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2827

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0A884

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0A884

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A884

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0207, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_021669_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A884

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A884

Family and domain databases

Conserved Domains Database

More...CDDi		cd00351, TS_Pyrimidine_HMase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.572.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00008, Thymidy_synth_bact, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR023451, Thymidate_synth/dCMP_Mease
IPR036926, Thymidate_synth/dCMP_Mease_sf
IPR000398, Thymidylate_synthase
IPR020940, Thymidylate_synthase_AS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00303, Thymidylat_synt, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00108, THYMDSNTHASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55831, SSF55831, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR03284, thym_sym, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00091, THYMIDYLATE_SYNTHASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0A884-1 [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 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0E6D88ED98D24D22
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

Protein sequence database of the Protein Information Resource

More...PIRi		A00549, SYECT

NCBI Reference Sequences

More...RefSeqi		NP_417304.1, NC_000913.3
WP_000816232.1, NZ_STEB01000034.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75866; AAC75866; b2827
BAE76896; BAE76896; BAE76896

Database of genes from NCBI RefSeq genomes

More...GeneIDi		61754179
949035

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2795
eco:b2827

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3908

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_000816232.1, NZ_STEB01000034.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
6CDZX-ray2.40A/B1-263[»]
6NNRX-ray1.05A/B1-264[»]
SMRiP0A884
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262058, 217 interactors
DIPiDIP-48261N
IntActiP0A884, 5 interactors
STRINGi511145.b2827

Chemistry databases

BindingDBiP0A884
ChEMBLiCHEMBL2555
DrugBankiDB02031, (6S)-5,6,7,8-tetrahydrofolic acid
DB04447, 1,4-Dithiothreitol
DB03541, 10-Propargyl-5,8-Dideazafolic Acid
DB03274, 2',5'-Dideoxyuridine
DB04457, 2'-Deoxyguanosine-5'-Monophosphate
DB02256, 2'-Deoxyuridine
DB08131, 2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID
DB04696, 4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN
DB02301, 5,10-Methylene-6-Hydrofolic Acid
DB03761, 5-fluoro-2'-deoxyuridine-5'-monophosphate
DB03800, Deoxyuridine monophosphate
DB02467, L-methionine (S)-S-oxide
DB02223, LY231514 tetra glu
DB03038, LY341770
DB03157, N,O-Didansyl-L-Tyrosine
DB03818, N-[Tosyl-D-Prolinyl]Amino-Ethanethiol
DB02899, N-Carboxymethionine
DB04586, o-Bromophenol
DB04530, S,S-(2-Hydroxyethyl)Thiocysteine
DB04503, Sp-722
DB03558, SP-876
DB02752, Tosyl-D-Proline
DrugCentraliP0A884

Proteomic databases

jPOSTiP0A884
PaxDbiP0A884
PRIDEiP0A884

Genome annotation databases

EnsemblBacteriaiAAC75866; AAC75866; b2827
BAE76896; BAE76896; BAE76896
GeneIDi61754179
949035
KEGGiecj:JW2795
eco:b2827
PATRICifig|1411691.4.peg.3908

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0995

Phylogenomic databases

eggNOGiCOG0207, Bacteria
HOGENOMiCLU_021669_0_0_6
InParanoidiP0A884
PhylomeDBiP0A884

Enzyme and pathway databases

UniPathwayiUPA00575
BioCyciEcoCyc:THYMIDYLATESYN-MONOMER
MetaCyc:THYMIDYLATESYN-MONOMER
BRENDAi2.1.1.45, 2026
SABIO-RKiP0A884

Miscellaneous databases

EvolutionaryTraceiP0A884

Protein Ontology

More...PROi		PR:P0A884

Family and domain databases

CDDicd00351, TS_Pyrimidine_HMase, 1 hit
Gene3Di3.30.572.10, 1 hit
HAMAPiMF_00008, Thymidy_synth_bact, 1 hit
InterProiView protein in InterPro
IPR023451, Thymidate_synth/dCMP_Mease
IPR036926, Thymidate_synth/dCMP_Mease_sf
IPR000398, Thymidylate_synthase
IPR020940, Thymidylate_synthase_AS
PfamiView protein in Pfam
PF00303, Thymidylat_synt, 1 hit
PRINTSiPR00108, THYMDSNTHASE
SUPFAMiSSF55831, SSF55831, 1 hit
TIGRFAMsiTIGR03284, thym_sym, 2 hits
PROSITEiView protein in PROSITE
PS00091, THYMIDYLATE_SYNTHASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTYSY_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A884
Secondary accession number(s): P00470, Q2MA10
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 2, 2021
This is version 137 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference 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
UniProt is an ELIXIR core data resource
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