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Entry version 142 (08 May 2019)
Sequence version 3 (15 Jul 1998)
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Protein

Sulfoquinovosidase

Gene

yihQ

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 hydrolysis of sulfoquinovosyl diacylglycerides (SQDG) to sulfoquinovose (SQ), which is then degraded by E.coli through the SQ Embden-Meyerhof-Parnas (SQ-EMP) sulfoglycolysis pathway as a source of carbon and sulfur. Therefore, is likely involved in the utilization of the sulfoquinovose headgroup found in ubiquitous plant sulfolipids. Is also able to hydrolyze simple sulfoquinovosides such as 1-sulfoquinovosylglycerol (SQGro). Is a retaining glycoside hydrolase, since it forms the alpha anomer of SQ (PubMed:26878550). Also exhibits some alpha-glucosidase activity against alpha-glucosyl fluoride in vitro, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed (PubMed:15294295).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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Is inactivated in vitro by the mechanism-based inactivator 5-fluoro-beta-L-idopyranosyl fluoride (5FIdoF) that yields a covalent glycosyl-enzyme complex with the active site nucleophile Asp-405.1 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 14.3 sec(-1) with para-nitrophenyl alpha-sulfoquinovoside as substrate.1 Publication
  1. KM=0.22 mM for para-nitrophenyl alpha-sulfoquinovoside1 Publication

    pH dependencei

    Optimum pH is 6.1 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: Glycolipid metabolism

    This protein is involved in Glycolipid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in Glycolipid 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 sitei288Substrate1 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 sitei405Nucleophile1 Publication1
    Active sitei408By similarity1
    Active sitei472Proton donor1 Publication1
    Binding sitei537Substrate1 Publication1

    <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 functionGlycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG11843-MONOMER
    ECOL316407:JW3849-MONOMER
    MetaCyc:EG11843-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P32138

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH31 Glycoside Hydrolase Family 31

    <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:
    Sulfoquinovosidase1 Publication (EC:3.2.1.1991 Publication)
    Short name:
    SQase1 Publication
    <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:yihQ1 PublicationImported
    Synonyms:squQImported
    Ordered Locus Names:b3878, JW3849
    <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
    EG11843 yihQ

    <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>Mutagenesisi288Q → E: Loss of catalytic activity against para-nitrophenyl alpha-sulfoquinovoside, but in contrast to wild-type, possesses a very weak alpha-glucosidase activity against para-nitrophenyl alpha-D-glucopyranoside. 1 Publication1
    Mutagenesisi301R → A or E: Loss of catalytic activity. 1 Publication1
    Mutagenesisi301R → K: Almost complete loss of catalytic activity. 1 Publication1
    Mutagenesisi301R → Q: 13-fold decrease in substrate affinity and 4600-fold decrease in catalytic activity. 1 Publication1
    Mutagenesisi304W → F: Loss of catalytic activity. 1 Publication1
    Mutagenesisi405D → A or N: Loss of catalytic activity. 1 Publication1
    Mutagenesisi472D → A or N: Loss of catalytic activity. 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_00001853721 – 678SulfoquinovosidaseAdd BLAST678

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P32138

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

    More...
    PaxDbi
    P32138

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P32138

    <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

    Induced during growth with sulfoquinovose.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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260866, 11 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-12498N

    Protein interaction database and analysis system

    More...
    IntActi
    P32138, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b3878

    <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

    1678
    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
    P32138

    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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni301 – 304Substrate binding1 Publication4

    <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 glycosyl hydrolase 31 family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CJQ Bacteria
    COG1501 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000064244

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P32138

    KEGG Orthology (KO)

    More...
    KOi
    K15922

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P32138

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.60.40.1180, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011013 Gal_mutarotase_sf_dom
    IPR000322 Glyco_hydro_31
    IPR013780 Glyco_hydro_b
    IPR017853 Glycoside_hydrolase_SF

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01055 Glyco_hydro_31, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51445 SSF51445, 1 hit
    SSF74650 SSF74650, 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.

    P32138-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MDTPRPQLLD FQFHQNNDSF TLHFQQRLIL THSKDNPCLW IGSGIADIDM
    60 70 80 90 100
    FRGNFSIKDK LQEKIALTDA IVSQSPDGWL IHFSRGSDIS ATLNISADDQ
    110 120 130 140 150
    GRLLLELQND NLNHNRIWLR LAAQPEDHIY GCGEQFSYFD LRGKPFPLWT
    160 170 180 190 200
    SEQGVGRNKQ TYVTWQADCK ENAGGDYYWT FFPQPTFVST QKYYCHVDNS
    210 220 230 240 250
    CYMNFDFSAP EYHELALWED KATLRFECAD TYISLLEKLT ALLGRQPELP
    260 270 280 290 300
    DWIYDGVTLG IQGGTEVCQK KLDTMRNAGV KVNGIWAQDW SGIRMTSFGK
    310 320 330 340 350
    RVMWNWKWNS ENYPQLDSRI KQWNQEGVQF LAYINPYVAS DKDLCEEAAQ
    360 370 380 390 400
    HGYLAKDASG GDYLVEFGEF YGGVVDLTNP EAYAWFKEVI KKNMIELGCG
    410 420 430 440 450
    GWMADFGEYL PTDTYLHNGV SAEIMHNAWP ALWAKCNYEA LEETGKLGEI
    460 470 480 490 500
    LFFMRAGSTG SQKYSTMMWA GDQNVDWSLD DGLASVVPAA LSLAMTGHGL
    510 520 530 540 550
    HHSDIGGYTT LFEMKRSKEL LLRWCDFSAF TPMMRTHEGN RPGDNWQFDG
    560 570 580 590 600
    DAETIAHFAR MTTVFTTLKP YLKEAVALNA KSGLPVMRPL FLHYEDDAHT
    610 620 630 640 650
    YTLKYQYLLG RDILVAPVHE EGRSDWTLYL PEDNWVHAWT GEAFRGGEVT
    660 670
    VNAPIGKPPV FYRADSEWAA LFASLKSI
    Length:678
    Mass (Da):77,275
    Last modified:July 15, 1998 - v3
    <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:i85869F52BB72FEE7
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti358A → R in AAB03011 (PubMed:8346018).Curated1
    Sequence conflicti517S → T in AAB03011 (PubMed:8346018).Curated1

    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
    L19201 Genomic DNA Translation: AAB03011.1
    U00096 Genomic DNA Translation: AAC76875.1
    AP009048 Genomic DNA Translation: BAE77431.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A65193

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418314.1, NC_000913.3
    WP_000380843.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76875; AAC76875; b3878
    BAE77431; BAE77431; BAE77431

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948376

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3849
    eco:b3878

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2833

    <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
    L19201 Genomic DNA Translation: AAB03011.1
    U00096 Genomic DNA Translation: AAC76875.1
    AP009048 Genomic DNA Translation: BAE77431.1
    PIRiA65193
    RefSeqiNP_418314.1, NC_000913.3
    WP_000380843.1, 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
    5AEDX-ray1.91A/B1-678[»]
    5AEEX-ray1.85A/B1-678[»]
    5AEGX-ray1.85A/B1-678[»]
    5OHTX-ray1.87A/B1-678[»]
    SMRiP32138
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4260866, 11 interactors
    DIPiDIP-12498N
    IntActiP32138, 1 interactor
    STRINGi511145.b3878

    Protein family/group databases

    CAZyiGH31 Glycoside Hydrolase Family 31

    Proteomic databases

    jPOSTiP32138
    PaxDbiP32138
    PRIDEiP32138

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76875; AAC76875; b3878
    BAE77431; BAE77431; BAE77431
    GeneIDi948376
    KEGGiecj:JW3849
    eco:b3878
    PATRICifig|1411691.4.peg.2833

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1789
    EcoGeneiEG11843 yihQ

    Phylogenomic databases

    eggNOGiENOG4105CJQ Bacteria
    COG1501 LUCA
    HOGENOMiHOG000064244
    InParanoidiP32138
    KOiK15922
    PhylomeDBiP32138

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11843-MONOMER
    ECOL316407:JW3849-MONOMER
    MetaCyc:EG11843-MONOMER
    SABIO-RKiP32138

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P32138

    Family and domain databases

    Gene3Di2.60.40.1180, 1 hit
    InterProiView protein in InterPro
    IPR011013 Gal_mutarotase_sf_dom
    IPR000322 Glyco_hydro_31
    IPR013780 Glyco_hydro_b
    IPR017853 Glycoside_hydrolase_SF
    PfamiView protein in Pfam
    PF01055 Glyco_hydro_31, 1 hit
    SUPFAMiSSF51445 SSF51445, 1 hit
    SSF74650 SSF74650, 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 nameiSQASE_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: P32138
    Secondary accession number(s): P76775, Q2M8H5
    <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: October 1, 1993
    Last sequence update: July 15, 1998
    Last modified: May 8, 2019
    This is version 142 of the entry and version 3 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. 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
    4. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    5. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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