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Entry version 78 (11 Dec 2019)
Sequence version 2 (04 Dec 2007)
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Protein

2-hydroxyethylphosphonate dioxygenase

Gene

hepD

Organism
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
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

Non-heme-dependent dioxygenase that catalyzes the conversion of 2-hydroxyethylphosphonate (HEP) to hydroxymethylphosphonate (HMP) in the biosynthesis of phosphinothricin tripeptide (PTT). PTT contains the unusual amino acid phosphinothricin attached to 2 alanine residues. Synthetic phosphinothricin (glufosinate) is a key component of commercial herbicides.5 Publications

Miscellaneous

Mediates the cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate (HEP) to produce hydroxymethylphosphonate (HMP) and formate without input of electrons or use of any organic cofactors. Reaction was initially supposed to follow a Criegee rearrangement with a phosphorus-based migrating group (PubMed:19839620). However, it was laster shown that it is not the case (PubMed:21381767).2 Publications
Phosphinothricin tripeptide (PTT) herbicide and fosfomycin antibiotic biosynthesis pathways share early steps starting with phosphoenolpyruvate before the pathways diverge after formation of 2-hydroxyethylphosphonate (HEP) (PubMed:17632514). HepD is involved in phosphinothricin tripeptide (PTT) herbicide biosynthesis after divergence of the 2 pathways (PubMed:19516340).2 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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

<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 0.35 sec(-1).
  1. KM=9.8 µM for 2-hydroxyethylphosphonate1 Publication
  2. KM=33 µM for O21 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: phosphonate biosynthesis

    This protein is involved in the pathway phosphonate biosynthesis, which is part of Phosphorus metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway phosphonate biosynthesis and in Phosphorus 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 sitei16Substrate; shared with dimeric partnerCombined sources1
    Binding sitei98SubstrateCombined sources1
    Binding sitei126SubstrateCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi129Iron; via tele nitrogenCombined sources2 Publications1
    Binding sitei176SubstrateCombined sources1
    Metal bindingi182Iron; via tele nitrogenCombined sources2 Publications1
    Binding sitei182SubstrateCombined sources1
    Binding sitei196SubstrateCombined sources1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi19 – 38H-T-H motifBy similarityAdd BLAST20
    DNA bindingi245 – 265H-T-H motifBy similarityAdd BLAST21

    <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

    GO - Biological processi

    <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 functionDioxygenase, DNA-binding, Oxidoreductase
    LigandIron, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-15041

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.13.11.72 6116

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

    More...
    UniPathwayi
    UPA00960

    <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:
    2-hydroxyethylphosphonate dioxygenase (EC:1.13.11.724 Publications)
    Alternative name(s):
    Hydroxyethylphosphonate dioxygenase
    Phosphinothricin tripeptide biosynthesis protein D
    <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:hepD
    Synonyms:phpD
    ORF Names:SSQG_01041
    <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>OrganismiStreptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
    <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 identifieri591159 [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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
    <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
    • UP000004184 <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: Unassembled WGS sequence

    <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>Mutagenesisi16K → A: Abolishes 2-hydroxyethylphosphonate dioxygenase activity. 1 Publication1
    Mutagenesisi90R → A: Results in a much higher apparent KM for 2-hydroxyethylphosphonate. Caanot be saturated in (O2). 1 Publication1
    Mutagenesisi98Y → F: Still able to convert 2-hydroxyethylphosphonate to hydroxymethylphosphonate and formate; however, in contrast to wild-type enzyme which consumes O(2) without a loss of catalytic activity, the rate of consumption of O(2) gradually decreases until the enzyme has lost all activity well before substrate has been consumed. 1 Publication1

    <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_00004220321 – 4432-hydroxyethylphosphonate dioxygenaseAdd BLAST443

    <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

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-15787755,EBI-15787755

    GO - Molecular functioni

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-59765N

    STRING: functional protein association networks

    More...
    STRINGi
    591159.ACEZ01000045_gene2950

    <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

    1443
    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
    Q5IW40

    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
    Q5IW40

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 63HTH cro/C1-type 1Add BLAST56
    Domaini234 – 290HTH cro/C1-type 2Add BLAST57

    <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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K12905

    Database of Orthologous Groups

    More...
    OrthoDBi
    603921at2

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.260.40, 2 hits
    2.60.120.10, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001387 Cro/C1-type_HTH
    IPR010982 Lambda_DNA-bd_dom_sf
    IPR014710 RmlC-like_jellyroll
    IPR011051 RmlC_Cupin_sf

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00530 HTH_XRE, 2 hits

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51182 SSF51182, 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.

    Q5IW40-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRIDPFKLAH WMNARKYTAA QTADLAGLPL DDLRRLLGDE ANEPDPAAAT
    60 70 80 90 100
    ALAEALSVEP SQLAADAHRN LTVVHKSAEE MHASRRPIQR DGIHFYNYYT
    110 120 130 140 150
    LAAPEGRVAP VVLDILCPSD RLPALNNGHL EPAITVNLGP GDINGRWGEE
    160 170 180 190 200
    ITPQTWRVLH ANHGGDRWIT GDSYVEPSYC PHSYSLAGDA PARIVSYTAQ
    210 220 230 240 250
    SNISPLMTEA NNWSTGAFEE ALKALSGKVS AGSVLDLFLA RRAHTRTSAA
    260 270 280 290 300
    EAAGVPPADL EAALRSPASE TGLTVLRTLG RALGFDYRVL LPADDQHDGV
    310 320 330 340 350
    GKTWTTIEDS RRSRRTFGTY EAASMASAAH LPDLVGSFLR VDADGRGADL
    360 370 380 390 400
    IDHAENHYVV TEGRLTLEWD GPDGPASVEL EPDGSAWTGP FVRHRWHGTG
    410 420 430 440
    TVLKFGSGAH LGYQDWLELT NTFEPAATLR RGRRDLAGWG YDN
    Length:443
    Mass (Da):48,091
    Last modified:December 4, 2007 - v2
    <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:i5ADBA86C73E65B48
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence CAJ14042 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    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
    X65195 Genomic DNA Translation: CAJ14042.1 Different initiation.
    AY632421 Genomic DNA Translation: AAU00079.2
    GG657757 Genomic DNA Translation: EFL30523.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_003988638.1, NZ_GG657757.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    EFL30523; EFL30523; SSQG_01041

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    34225385

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:AAU00079

    <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
    X65195 Genomic DNA Translation: CAJ14042.1 Different initiation.
    AY632421 Genomic DNA Translation: AAU00079.2
    GG657757 Genomic DNA Translation: EFL30523.1
    RefSeqiWP_003988638.1, NZ_GG657757.1

    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
    3G7DX-ray1.80A1-443[»]
    3GBFX-ray1.92A1-443[»]
    3RZZX-ray2.20A1-443[»]
    4YARX-ray1.75A1-443[»]
    SMRiQ5IW40
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    DIPiDIP-59765N
    STRINGi591159.ACEZ01000045_gene2950

    Genome annotation databases

    EnsemblBacteriaiEFL30523; EFL30523; SSQG_01041
    GeneIDi34225385
    KEGGiag:AAU00079

    Phylogenomic databases

    KOiK12905
    OrthoDBi603921at2

    Enzyme and pathway databases

    UniPathwayiUPA00960
    BioCyciMetaCyc:MONOMER-15041
    BRENDAi1.13.11.72 6116

    Miscellaneous databases

    EvolutionaryTraceiQ5IW40

    Family and domain databases

    Gene3Di1.10.260.40, 2 hits
    2.60.120.10, 2 hits
    InterProiView protein in InterPro
    IPR001387 Cro/C1-type_HTH
    IPR010982 Lambda_DNA-bd_dom_sf
    IPR014710 RmlC-like_jellyroll
    IPR011051 RmlC_Cupin_sf
    SMARTiView protein in SMART
    SM00530 HTH_XRE, 2 hits
    SUPFAMiSSF51182 SSF51182, 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 nameiHEPD_STRVT
    <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: Q5IW40
    Secondary accession number(s): D9XF44, Q4JFE9
    <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: April 3, 2013
    Last sequence update: December 4, 2007
    Last modified: December 11, 2019
    This is version 78 of the entry and version 2 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

    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
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