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UniProtKB - P05794 (DYR23_ECOLX)

Entry version 93 (31 Jul 2019)
Sequence version 1 (01 Nov 1988)
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Protein

Dihydrofolate reductase type 2

Gene
N/A
Organism
Escherichia coli
Status
Reviewed-Annotation score:

Annotation score:3 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>-Protein inferred from homologyi <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

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).By similarity

Miscellaneous

Type II plasmid-specified enzyme is practically insensitive to trimethoprim and methotrexate.

<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 <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: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydrofolate reductase (D4587_00460), Dihydrofolate reductase type 8 (dhfrVIII), Dihydrofolate reductase type 9 (dhfrIX), Dihydrofolate reductase (BTQ06_28630), Dihydrofolate reductase, Dihydrofolate reductase (APZ14_00990), Dihydrofolate reductase (dfrB2), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase type A10 (dfrA10), Dihydrofolate reductase (dfrA21), Dihydrofolate reductase (C9Y95_01915), Dihydrofolate reductase (folA), Dihydrofolate reductase (C9224_00785), Dihydrofolate reductase (dfr2d), Dihydrofolate reductase (D9F05_04510), Dihydrofolate reductase (C5715_27395), Dihydrofolate reductase (DUM94_12960), Dihydrofolate reductase type 2, Dihydrofolate reductase (dfrB3), Dihydrofolate reductase type 2, Dihydrofolate reductase type 1 (dhfrI), Dihydrofolate reductase (DS143_29305), Dihydrofolate reductase (C9003_10310), Dihydrofolate reductase type 5 (dhfrV), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (DXF93_00550), Dihydrofolate reductase type 15 (dhfrXV), Dihydrofolate reductase (dfrII), Dihydrofolate reductase (D9J03_00795), Dihydrofolate reductase (EBA78_10940), Dihydrofolate reductase (D7Z87_07315), Dihydrofolate reductase (BHS87_26495), Dihydrofolate reductase (ECs0051), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfrA26), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (CI641_024860), Dihydrofolate reductase (dfr2d), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase type A13 (dfrA13), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase type 2, Dihydrofolate reductase (C9108_15520), Dihydrofolate reductase (CSB64_27845), Dihydrofolate reductase (C9175_03430), Dihydrofolate reductase (dfr2a), Dihydrofolate reductase type 7 (dhfrVII), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (folA_2), Dihydrofolate reductase (dfr22), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfr22), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (folA)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

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 sitei32NADPBy similarity1
Binding sitei68Substrate; via amide nitrogenBy similarity1

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 bindingi66 – 69NADPBy similarity4

<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 functionOxidoreductase
Biological processAntibiotic resistance, Methotrexate resistance, One-carbon metabolism, Trimethoprim resistance
LigandNADP

Enzyme and pathway databases

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

More...UniPathwayi		UPA00077;UER00158

<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:
Dihydrofolate reductase type 2 (EC:1.5.1.3)
Alternative name(s):
Dihydrofolate reductase type II
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid IncP-beta R7510 Publication
<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
<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 identifieri562 [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 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001864371 – 78Dihydrofolate reductase type 2Add BLAST78

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P05794

<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

Homotetramer.

By similarity

<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

3D structure databases

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

More...SMRi		P05794

Database of comparative protein structure models

More...ModBasei		Search...

<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 general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The active site is situated at the inner surface of a pore formed by the four subunits.By similarity

Phylogenomic databases

KEGG Orthology (KO)

More...KOi		K19645

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.30.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009159 Dhfr_type_II
IPR008990 Elect_transpt_acc-like_dom_sf
IPR023408 MscS_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF06442 DHFR_2, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000199 Dhfr_type_II, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50090 SSF50090, 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.

P05794-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDQHNNGVST LVAGQFALPS HATFGLGDRV RKKSGAAWQG QVVGWYCTKL 
        60         70 
TPEGYAVESE SHPGSVQIYP VAALERVA
Length:78
Mass (Da):8,328
Last modified:November 1, 1988 - 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:i3D67C2EB67220697
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
X04128 Genomic DNA Translation: CAA27740.1
X72585 Genomic DNA Translation: CAA51181.1
U67194 Genomic DNA Translation: AAC64461.1

Protein sequence database of the Protein Information Resource

More...PIRi		A23598 RDECD5
S32183

NCBI Reference Sequences

More...RefSeqi		WP_010890144.1, NZ_UNPX01000121.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		39490308

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ag:CAA51181

<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
X04128 Genomic DNA Translation: CAA27740.1
X72585 Genomic DNA Translation: CAA51181.1
U67194 Genomic DNA Translation: AAC64461.1
PIRiA23598 RDECD5
S32183
RefSeqiWP_010890144.1, NZ_UNPX01000121.1

3D structure databases

SMRiP05794
ModBaseiSearch...

Proteomic databases

PRIDEiP05794

Genome annotation databases

GeneIDi39490308
KEGGiag:CAA51181

Phylogenomic databases

KOiK19645

Enzyme and pathway databases

UniPathwayiUPA00077;UER00158

Family and domain databases

Gene3Di2.30.30.60, 1 hit
InterProiView protein in InterPro
IPR009159 Dhfr_type_II
IPR008990 Elect_transpt_acc-like_dom_sf
IPR023408 MscS_dom_sf
PfamiView protein in Pfam
PF06442 DHFR_2, 1 hit
PIRSFiPIRSF000199 Dhfr_type_II, 1 hit
SUPFAMiSSF50090 SSF50090, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiDYR23_ECOLX
<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: P05794
<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: November 1, 1988
Last sequence update: November 1, 1988
Last modified: July 31, 2019
This is version 93 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

Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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