Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 87 (11 Dec 2019)
Sequence version 1 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Sucrose phosphorylase

Gene

sucP

Organism
Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
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 reversible phosphorolysis of sucrose into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189, PubMed:20691225). Is involved in sucrose degradation. Also displays transglucosylation activity in vitro, by transferring the glucosyl moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-arabinose, D- and L-arabitol, and xylitol (PubMed:14740189).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 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 207 sec(-1) for the phosphorolysis of sucrose (at 58 degrees Celsius and pH 6.5).1 Publication
  1. KM=6.8 mM for sucrose (at 58 degrees Celsius and pH 6.5)1 Publication

    pH dependencei

    Optimum pH is 6.0-6.5 for the phosphorolysis of sucrose.2 Publications

    Temperature dependencei

    Optimum temperature is 48 degrees Celsius for the phosphorolysis of sucrose (PubMed:14740189). The His-tagged enzyme shows an optimum temperature of 58 degrees Celsius (PubMed:20691225). The immobilization of the enzyme on Sepabeads EC-HFA increases thermostability, and optimum temperature is shifted to 65 degrees Celsius (PubMed:20691225).2 Publications

    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 sitei50SubstrateCombined sources1 Publication1
    Binding sitei88SubstrateCombined sources1 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 sitei192Nucleophile1 Publication1 Publication1
    Active sitei232Proton donor2 Publications1
    Binding sitei232SubstrateCombined sources1 Publication1
    Binding sitei399SubstrateCombined sources1 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 functionGlycosyltransferase, Transferase
    Biological processCarbohydrate metabolism

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    BADO367928:G1G2R-86-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.4.1.7 842

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH13 Glycoside Hydrolase Family 13

    <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:
    Sucrose phosphorylase3 Publications (EC:2.4.1.72 Publications)
    Short name:
    SP1 Publication
    Short name:
    SPase1 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:sucP1 Publication
    Synonyms:splImported
    Ordered Locus Names:BAD_0078Imported
    <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>OrganismiBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
    <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 identifieri367928 [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 lineageiBacteriaActinobacteriaBifidobacterialesBifidobacteriaceaeBifidobacterium
    <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
    • UP000008702 <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 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>Mutagenesisi232E → Q: Loss of catalytic activity. 1 Publication1
    Mutagenesisi345Q → F: Decreases affinity for sucrose. Highly improves in vitro activity towards aromatic acceptors, allowing efficient glucosylation of resveratrol, (+)-catechin and (-)-epicatechin. 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_00004424351 – 504Sucrose phosphorylaseAdd BLAST504

    <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 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

    1504
    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
    A0ZZH6

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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>Regioni190 – 192Substrate bindingCombined sources1 Publication3
    Regioni289 – 290Substrate bindingCombined sources1 Publication2
    Regioni342 – 345Substrate bindingCombined sources1 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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4107RK0 Bacteria
    COG0366 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000220752

    KEGG Orthology (KO)

    More...
    KOi
    K00690

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NFTASHD

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd11355 AmyAc_Sucrose_phosphorylase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006047 Glyco_hydro_13_cat_dom
    IPR017853 Glycoside_hydrolase_SF
    IPR015325 Suc_Porlyase_C
    IPR016377 Sucrose_GGa_phosphorylase-rel
    IPR022527 Sucrose_phospho

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00128 Alpha-amylase, 1 hit
    PF09244 DUF1964, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF003059 Sucrose_phosphorylase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00642 Aamy, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51445 SSF51445, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03852 sucrose_gtfA, 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.

    A0ZZH6-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKNKVQLITY ADRLGDGTIK SMTDILRTRF DGVYDGVHIL PFFTPFDGAD
    60 70 80 90 100
    AGFDPIDHTK VDERLGSWDD VAELSKTHNI MVDAIVNHMS WESKQFQDVL
    110 120 130 140 150
    AKGEESEYYP MFLTMSSVFP NGATEEDLAG IYRPRPGLPF THYKFAGKTR
    160 170 180 190 200
    LVWVSFTPQQ VDIDTDSDKG WEYLMSIFDQ MAASHVSYIR LDAVGYGAKE
    210 220 230 240 250
    AGTSCFMTPK TFKLISRLRE EGVKRGLEIL IEVHSYYKKQ VEIASKVDRV
    260 270 280 290 300
    YDFALPPLLL HALSTGHVEP VAHWTDIRPN NAVTVLDTHD GIGVIDIGSD
    310 320 330 340 350
    QLDRSLKGLV PDEDVDNLVN TIHANTHGES QAATGAAASN LDLYQVNSTY
    360 370 380 390 400
    YSALGCNDQH YIAARAVQFF LPGVPQVYYV GALAGKNDME LLRKTNNGRD
    410 420 430 440 450
    INRHYYSTAE IDENLKRPVV KALNALAKFR NELDAFDGTF SYTTDDDTSI
    460 470 480 490 500
    SFTWRGETSQ ATLTFEPKRG LGVDNTTPVA MLEWEDSAGD HRSDDLIANP

    PVVA
    Length:504
    Mass (Da):56,190
    Last modified:January 23, 2007 - 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:i10705FE3182E5754
    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
    AF543301 Genomic DNA Translation: AAO33821.1
    AP009256 Genomic DNA Translation: BAF38859.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011742626.1, NC_008618.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAF38859; BAF38859; BAD_0078

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    4556453

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bad:BAD_0078

    <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
    AF543301 Genomic DNA Translation: AAO33821.1
    AP009256 Genomic DNA Translation: BAF38859.1
    RefSeqiWP_011742626.1, NC_008618.1

    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
    1R7AX-ray1.77A/B1-504[»]
    2GDUX-ray2.10A/B1-504[»]
    2GDVX-ray2.00A/B1-504[»]
    5C8BX-ray2.70B1-504[»]
    5M9XX-ray2.35B1-504[»]
    5MANX-ray2.04B1-504[»]
    5MB2X-ray1.75B1-504[»]
    6FMEX-ray1.51A/B1-504[»]
    SMRiA0ZZH6
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    CAZyiGH13 Glycoside Hydrolase Family 13

    Genome annotation databases

    EnsemblBacteriaiBAF38859; BAF38859; BAD_0078
    GeneIDi4556453
    KEGGibad:BAD_0078

    Phylogenomic databases

    eggNOGiENOG4107RK0 Bacteria
    COG0366 LUCA
    HOGENOMiHOG000220752
    KOiK00690
    OMAiNFTASHD

    Enzyme and pathway databases

    BioCyciBADO367928:G1G2R-86-MONOMER
    BRENDAi2.4.1.7 842

    Family and domain databases

    CDDicd11355 AmyAc_Sucrose_phosphorylase, 1 hit
    InterProiView protein in InterPro
    IPR006047 Glyco_hydro_13_cat_dom
    IPR017853 Glycoside_hydrolase_SF
    IPR015325 Suc_Porlyase_C
    IPR016377 Sucrose_GGa_phosphorylase-rel
    IPR022527 Sucrose_phospho
    PfamiView protein in Pfam
    PF00128 Alpha-amylase, 1 hit
    PF09244 DUF1964, 1 hit
    PIRSFiPIRSF003059 Sucrose_phosphorylase, 1 hit
    SMARTiView protein in SMART
    SM00642 Aamy, 1 hit
    SUPFAMiSSF51445 SSF51445, 1 hit
    TIGRFAMsiTIGR03852 sucrose_gtfA, 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 nameiSUCP_BIFAA
    <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: A0ZZH6
    Secondary accession number(s): Q84HQ2
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2017
    Last sequence update: January 23, 2007
    Last modified: December 11, 2019
    This is version 87 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, Direct protein sequencing, 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again