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Entry version 59 (11 Dec 2019)
Sequence version 1 (10 Jun 2008)
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Protein

Polysaccharide lyase

Gene

Smlt1473

Organism
Stenotrophomonas maltophilia (strain K279a)
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

Polysaccharide lyase that catalyzes the depolymerization of several anionic polysaccharides via a beta-elimination mechanism. Exhibits broad substrate specificity, catalyzing the degradation of not only alginate and poly-beta-D-mannuronate (poly-ManA), but poly-beta-D-glucuronate (poly-GlcA or poly-GlcUA) and hyaluronate (HA) as well. The oligosaccharide products formed by enzymatic cleavage are comprised mainly of disaccharides, with a lower abundance of trimers and pentamers. Is not active on poly-D-galacturonate, heparin and heparin sulfate.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

  • Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.1 Publication EC:4.2.2.3
  • Eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.1 Publication EC:4.2.2.14

<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 inhibited by mono- and divalent cations as well as L-ascorbic acid 6-hexadecanoate.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

Vmax for poly-GlcA is about 10-fold greater versus poly-ManA or HA (PubMed:24257754). kcat is 31.9 sec(-1) with poly-GlcA as substrate (at pH 7) (PubMed:24808176). kcat is 3.3 sec(-1) with poly-ManA as substrate (at pH 9) (PubMed:24808176).2 Publications
  1. KM=0.14 mg/ml for poly-GlcA1 Publication
  2. KM=0.26 mg/ml for poly-ManA1 Publication
  3. KM=0.55 mg/ml for hyaluronan1 Publication
  4. KM=0.17 mM for poly-GlcA (at pH 7)1 Publication
  5. KM=0.35 mM for poly-ManA (at pH 9)1 Publication

    pH dependencei

    Optimum pH for enzymatic activity is substrate-dependent, with optimal hyaluronate degradation at pH 5, poly-beta-D-glucuronate degradation at pH 7, and alginate degradation at pH 9.1 Publication

    <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 functionLyase
    Biological processCarbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    SMAL522373:SMLT_RS07070_1-MONOMER

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    PL5 Polysaccharide Lyase Family 5

    <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:
    Polysaccharide lyase1 Publication (EC:4.2.2.-1 Publication)
    Short name:
    PL1 Publication
    Alternative name(s):
    Alginate lyase1 Publication (EC:4.2.2.31 Publication)
    Endolytic polysaccharide lyaseCurated
    Hyaluronate lyase1 Publication (EC:4.2.2.11 Publication)
    Multifunctional polysaccharide lyase1 Publication
    Poly-beta-D-glucuronate lyase1 Publication (EC:4.2.2.141 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
    Ordered Locus Names:Smlt1473
    <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>OrganismiStenotrophomonas maltophilia (strain K279a)
    <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 identifieri522373 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
    <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
    • UP000008840 <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

    <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

    • Cell outer membrane 1 Publication; Lipid-anchor PROSITE-ProRule annotation1 Publication

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    <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>Mutagenesisi23C → F: Impairs subcellular location since the protein mutant is completely retained in the cytosol. Loss of extracellular lyase activity in mutant cells. 1 Publication1
    Mutagenesisi167N → L: Less than 0.5% of wild-type activity against all substrates. 1 Publication1
    Mutagenesisi168H → A: Retains 10% of activity toward poly-GlcA, but shows less than 0.5% of wild-type activity against poly-ManA and HA. 1 Publication1
    Mutagenesisi171W → A: Displays nearly eliminated HA activity, while increasing poly-ManA and poly-GlcA activity by at least 35%. 1 Publication1
    Mutagenesisi215R → L: Less than 0.5% of wild-type activity against all substrates. 1 Publication1
    Mutagenesisi221H → F: Increases activity and specificity toward poly-ManA. 1 Publication1
    Mutagenesisi222Y → F: Less than 0.5% of wild-type activity against all substrates. 1 Publication1
    Mutagenesisi312R → L: Increases activity and specificity toward poly-GlcA. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22CuratedAdd BLAST22
    <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_500034177823 – 331Polysaccharide lyaseAdd BLAST309

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi23N-palmitoyl cysteineCurated1
    Lipidationi23S-diacylglycerol cysteineCurated1

    Keywords - PTMi

    Lipoprotein, Palmitate

    <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

    STRING: functional protein association networks

    More...
    STRINGi
    522373.Smlt1473

    <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
    B2FHL8

    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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the polysaccharide lyase 5 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105FN4 Bacteria
    ENOG4111N6J LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000056685

    KEGG Orthology (KO)

    More...
    KOi
    K01729

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    AAWSVMA

    Database of Orthologous Groups

    More...
    OrthoDBi
    804604at2

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.50.10.100, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008397 Alginate_lyase_dom
    IPR008929 Chondroitin_lyas

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF05426 Alginate_lyase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48230 SSF48230, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51257 PROKAR_LIPOPROTEIN, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    B2FHL8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSLPLRLALL PTLLASASAF AACPAPPPGQ PDIRAIGYYT DKAGSVIDPA
    60 70 80 90 100
    LQQQNKDATA PLDRYAADVA RMSDDYLRNG DPAAAQCTLS WLGAWADDGA
    110 120 130 140 150
    MLGQMIRVNN DQSFYMRQWM LDAVAMAYLK VHDQANPQQR ARIDPWLQKL
    160 170 180 190 200
    ARANLAYWDN PKRRRNNHYY WGGLGVLATG LATDDDALWQ AGHAAFQKGI
    210 220 230 240 250
    DDIQDDGSLP LEMARGQRAL HYHDYALAPL VMMAELARLR GQDWYASRNH
    260 270 280 290 300
    AIDRLARRVI EGSRDPAWFN QHTGAAQLPL QASGWVEFYR LRSPDGGVFD
    310 320 330
    AAHARGPFHS PRLGGDLTLM ATHGIVRTPL R
    Length:331
    Mass (Da):36,696
    Last modified:June 10, 2008 - 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:iB3D40DDFE2714589
    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
    AM743169 Genomic DNA Translation: CAQ45011.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_012479599.1, NC_010943.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAQ45011; CAQ45011; Smlt1473

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    6395630

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sml:Smlt1473

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|522373.3.peg.1413

    <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
    AM743169 Genomic DNA Translation: CAQ45011.1
    RefSeqiWP_012479599.1, NC_010943.1

    3D structure databases

    SMRiB2FHL8
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi522373.Smlt1473

    Protein family/group databases

    CAZyiPL5 Polysaccharide Lyase Family 5

    Genome annotation databases

    EnsemblBacteriaiCAQ45011; CAQ45011; Smlt1473
    GeneIDi6395630
    KEGGisml:Smlt1473
    PATRICifig|522373.3.peg.1413

    Phylogenomic databases

    eggNOGiENOG4105FN4 Bacteria
    ENOG4111N6J LUCA
    HOGENOMiHOG000056685
    KOiK01729
    OMAiAAWSVMA
    OrthoDBi804604at2

    Enzyme and pathway databases

    BioCyciSMAL522373:SMLT_RS07070_1-MONOMER

    Family and domain databases

    Gene3Di1.50.10.100, 1 hit
    InterProiView protein in InterPro
    IPR008397 Alginate_lyase_dom
    IPR008929 Chondroitin_lyas
    PfamiView protein in Pfam
    PF05426 Alginate_lyase, 1 hit
    SUPFAMiSSF48230 SSF48230, 1 hit
    PROSITEiView protein in PROSITE
    PS51257 PROKAR_LIPOPROTEIN, 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 nameiPL_STRMK
    <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: B2FHL8
    <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 9, 2014
    Last sequence update: June 10, 2008
    Last modified: December 11, 2019
    This is version 59 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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