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Protein

5,10-methylenetetrahydrofolate reductase

Gene

metF

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

Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.1 Publication

<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

FAD6 Publications

<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

  1. KM=17 µM for NADPH2 Publications
  2. KM=3.9 µM for 5,10-methylenetetrahydrofolate2 Publications

    pH dependencei

    Optimum pH is 6.3-6.4.2 Publications

    <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 interconversion

    This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
    View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei28Proton donor/acceptor2 Publications1
    <p>This subsection of the ‘Function’ 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 sitei88FAD2 Publications1
    Binding sitei120Substrate1
    Binding sitei152FAD2 Publications1
    Binding sitei183Substrate1
    Binding sitei219Substrate1
    Binding sitei223Substrate1
    Binding sitei275Substrate1
    Binding sitei279Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi28 – 33NAD6
    Nucleotide bindingi59 – 62FAD2 Publications4
    Nucleotide bindingi59 – 60NAD2
    Nucleotide bindingi118 – 120FAD2 Publications3
    Nucleotide bindingi131 – 132FAD2 Publications2
    Nucleotide bindingi156 – 159FAD2 Publications4
    Nucleotide bindingi165 – 172FAD2 Publications8

    <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

    • FAD binding Source: EcoCyc
    • methylenetetrahydrofolate reductase (NAD(P)H) activity Source: EcoCyc

    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 functionOxidoreductase
    Biological processAmino-acid biosynthesis, Methionine biosynthesis
    LigandFAD, Flavoprotein, NAD, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.5.1.20 2026

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

    More...
    UniPathwayi
    UPA00193

    <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:
    5,10-methylenetetrahydrofolate reductase (EC:1.5.1.20)
    <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:metF
    Ordered Locus Names:b3941, JW3913
    <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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10585 metF

    <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

    GO - Cellular componenti

    • cytosol Source: GO_Central

    <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>Mutagenesisi28E → Q: Abolishes enzyme activity. 2 Publications1
    Mutagenesisi120D → N: Strongly reduces enzyme activity. Strongly reduces affinity for 5-methyltetrahydrofolate. 1 Publication1
    Mutagenesisi177A → V: Increases the propensity to lose its essential flavin cofactor. 1 Publication1
    Mutagenesisi223F → A: Strongly decreases substrate and NADH binding. 1 Publication1
    Mutagenesisi223F → L: Slightly reduced enzyme activity. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03147 Flavin adenine dinucleotide

    <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_00001902611 – 2965,10-methylenetetrahydrofolate reductaseAdd BLAST296

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0AEZ1

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

    More...
    PaxDbi
    P0AEZ1

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0AEZ1

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Repressed by methionine.1 Publication

    <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.3 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263063, 24 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-6848N

    Protein interaction database and analysis system

    More...
    IntActi
    P0AEZ1, 4 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_4130

    <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

    1296
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P0AEZ1

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

    More...
    SMRi
    P0AEZ1

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0AEZ1

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105SYT Bacteria
    COG0685 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000246232

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0AEZ1

    KEGG Orthology (KO)

    More...
    KOi
    K00297

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0AEZ1

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00537 MTHFR, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029041 FAD-linked_oxidoreductase-like
    IPR003171 Mehydrof_redctse
    IPR004620 MTHF_reductase_bac

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02219 MTHFR, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51730 SSF51730, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00676 fadh2, 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>.<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.

    P0AEZ1-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSFFHASQRD ALNQSLAEVQ GQINVSFEFF PPRTSEMEQT LWNSIDRLSS
    60 70 80 90 100
    LKPKFVSVTY GANSGERDRT HSIIKGIKDR TGLEAAPHLT CIDATPDELR
    110 120 130 140 150
    TIARDYWNNG IRHIVALRGD LPPGSGKPEM YASDLVTLLK EVADFDISVA
    160 170 180 190 200
    AYPEVHPEAK SAQADLLNLK RKVDAGANRA ITQFFFDVES YLRFRDRCVS
    210 220 230 240 250
    AGIDVEIIPG ILPVSNFKQA KKFADMTNVR IPAWMAQMFD GLDDDAETRK
    260 270 280 290
    LVGANIAMDM VKILSREGVK DFHFYTLNRA EMSYAICHTL GVRPGL
    Length:296
    Mass (Da):33,103
    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:iB702702D2BE9521E
    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
    V01502 Genomic DNA Translation: CAA24747.1
    L19201 Genomic DNA Translation: AAB03073.1
    U00096 Genomic DNA Translation: AAC76923.1
    AP009048 Genomic DNA Translation: BAE77369.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A00462 RDECMH

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418376.1, NC_000913.3
    WP_000007523.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76923; AAC76923; b3941
    BAE77369; BAE77369; BAE77369

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948432

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3913
    eco:b3941

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2763

    <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
    V01502 Genomic DNA Translation: CAA24747.1
    L19201 Genomic DNA Translation: AAB03073.1
    U00096 Genomic DNA Translation: AAC76923.1
    AP009048 Genomic DNA Translation: BAE77369.1
    PIRiA00462 RDECMH
    RefSeqiNP_418376.1, NC_000913.3
    WP_000007523.1, NZ_LN832404.1

    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
    1B5TX-ray2.50A/B/C21-294[»]
    1ZP3X-ray1.85A/B/C1-296[»]
    1ZP4X-ray1.85A/B/C1-296[»]
    1ZPTX-ray1.95A/B/C1-296[»]
    1ZRQX-ray2.20A/B/C1-296[»]
    2FMNX-ray2.05A/B/C1-296[»]
    2FMOX-ray2.25A/B/C1-296[»]
    3FSTX-ray1.65A/C/E1-296[»]
    3FSUX-ray1.70A/C/E1-296[»]
    ProteinModelPortaliP0AEZ1
    SMRiP0AEZ1
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263063, 24 interactors
    DIPiDIP-6848N
    IntActiP0AEZ1, 4 interactors
    STRINGi316385.ECDH10B_4130

    Chemistry databases

    DrugBankiDB03147 Flavin adenine dinucleotide

    Proteomic databases

    EPDiP0AEZ1
    PaxDbiP0AEZ1
    PRIDEiP0AEZ1

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76923; AAC76923; b3941
    BAE77369; BAE77369; BAE77369
    GeneIDi948432
    KEGGiecj:JW3913
    eco:b3941
    PATRICifig|1411691.4.peg.2763

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0580
    EcoGeneiEG10585 metF

    Phylogenomic databases

    eggNOGiENOG4105SYT Bacteria
    COG0685 LUCA
    HOGENOMiHOG000246232
    InParanoidiP0AEZ1
    KOiK00297
    PhylomeDBiP0AEZ1

    Enzyme and pathway databases

    UniPathwayi
    UPA00193

    BioCyciEcoCyc:METHYLENETHFREDUCT-MONOMER
    MetaCyc:METHYLENETHFREDUCT-MONOMER
    BRENDAi1.5.1.20 2026

    Miscellaneous databases

    EvolutionaryTraceiP0AEZ1

    Protein Ontology

    More...
    PROi
    PR:P0AEZ1

    Family and domain databases

    CDDicd00537 MTHFR, 1 hit
    InterProiView protein in InterPro
    IPR029041 FAD-linked_oxidoreductase-like
    IPR003171 Mehydrof_redctse
    IPR004620 MTHF_reductase_bac
    PfamiView protein in Pfam
    PF02219 MTHFR, 1 hit
    SUPFAMiSSF51730 SSF51730, 1 hit
    TIGRFAMsiTIGR00676 fadh2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiMETF_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: P0AEZ1
    Secondary accession number(s): P00394, Q2M8N7
    <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: December 5, 2018
    This is version 109 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, Complete proteome, Reference proteome

    Documents

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