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UniProtKB - E4PMA5 (GGOP_MARAH)

Entry version 58 (02 Dec 2020)
Sequence version 1 (08 Feb 2011)
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Protein

Glucosylglycerol phosphorylase

Gene

gtfA

Organism
Marinobacter adhaerens (strain DSM 23420 / HP15)
Status
Reviewed-Annotation score:

Annotation score:4 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 2-O-alpha-D-glucosylglycerol with retention of the anomeric configuration, forming alpha-D-glucose 1-phosphate and glycerol. Has most likely a catabolic role, either regulating the intracellular levels of glucosylglycerol, which acts as a compatible solute, or degrading it when the environmental conditions change. Cannot catalyze the phosphorolysis of sucrose or glucosylglycerate.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 14 sec(-1) towards 2-O-(alpha-D-glucopyranosyl)glycerol for the phosphorolytic direction (at pH 6.5 and 37 degrees Celsius). kcat is 14 sec(-1) towards phosphate for the phosphorolytic direction (at pH 6.5 and 37 degrees Celsius). kcat is 36 sec(-1) towards alpha-D-glucose 1-phosphate for the synthetic direction (at pH 6.5 and 37 degrees Celsius). kcat is 39 sec(-1) towards glycerol for the synthetic direction (at pH 6.5 and 37 degrees Celsius).1 Publication
  1. KM=3.9 mM for 2-O-(alpha-D-glucopyranosyl)glycerol (at pH 6.5 and 37 degrees Celsius)1 Publication
  2. KM=10 mM for phosphate (at pH 6.5 and 37 degrees Celsius)1 Publication
  3. KM=2.5 mM for alpha-D-glucose 1-phosphate (at pH 6.5 and 37 degrees Celsius)1 Publication
  4. KM=7.0 mM for glycerol (at pH 6.5 and 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius. Full activity is retained after incubating at up to 45 degrees Celsius for 10 minutes, while only 46% is left after incubating at 50 degrees Celsius. The protein is completely denatured after incubating at higher temperatures.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei190NucleophileBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei194Substrate1 Publication1
    Active sitei231Proton donorBy similarity1
    Binding sitei336Substrate1 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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    		MADH225937:G1GOU-2842-MONOMER
    MetaCyc:MONOMER-20515

    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%5Fand%5Ftaxonomy%5Fsection">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:
    Glucosylglycerol phosphorylase1 Publication (EC:2.4.1.3591 Publication)
    Short name:
    GGoP1 Publication
    Alternative name(s):
    2-O-alpha-D-glucopyranosylglycerol:phosphate alpha-D-glucosyltransferase1 Publication
    2-O-alpha-D-glucosylglycerol phosphorylase (retaining)1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:gtfAImported
    Ordered Locus Names:HP15_2853Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMarinobacter adhaerens (strain DSM 23420 / HP15)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri225937 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Marinobacter ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000007077 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Might be an attractive biocatalyst for the production of the osmolyte glucosylglycerol, which is currently produced on industrial scale by exploiting a side activity of the closely related sucrose phosphorylase. GGoP from M.adhaerens may offer far higher productivities due to its high specific activity in the synthesis direction. Glucosylglycerol is commercially distributed as a moisturising agent in cosmetics and can also serve as a stabilizing agent in protein formulations, or even as a functional food.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi194Y → A: 2.7% of wild-type catalytic activity. 1 Publication1
    Mutagenesisi333A → D: 0.3% of wild-type catalytic activity. Does not gain activity on sucrose. 1 Publication1
    Mutagenesisi336Q → A: 2.6% of wild-type 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004440461 – 480Glucosylglycerol phosphorylaseAdd BLAST480

    <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    		225937.HP15_2853

    <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    		E4PMA5

    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 glycosyl hydrolase 13 family. Sucrose phosphorylase subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0366, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_021358_1_0_6

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		CFMLEET

    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
    IPR016377, Sucrose_GGa_phosphorylase-rel
    IPR022527, Sucrose_phospho

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00128, Alpha-amylase, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    E4PMA5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLLKNAVQLI CYPDRIGNNL KDLYTVVDTH LSEAIGGLHI LPFFPSNADG 
            60         70         80         90        100
    GFSPLTHKEV DPKVGTWDDI EAFTAKYDLC VDLTVNHISD ESPEFTDFIA 
           110        120        130        140        150
    NGFDSEYADL FVHVDKFGEI SPDDMAKIHI RKEKEPFREV TLSDGTKTRV 
           160        170        180        190        200
    WCTFTEQQID LNYESDLAYQ LMESYIGFLT SKGVNLLRLD AFGYTTKRIG 
           210        220        230        240        250
    TSCFLVEPEV YQILDWVNQV ALKHGAECLP EVHDHTSYQY AISRRNMHPY 
           260        270        280        290        300
    GFALPPLLLY SLLDANSTYL KNWLRMCPRN MVTVLDTHDG ICIPDVEGVL 
           310        320        330        340        350
    PDEKIKVLID NIDARSADPI MRRSAANIHS VGAIYQLTCT FYDALMQNDD 
           360        370        380        390        400
    AYIAARAIQF FTPGIPQVYY VGLLAGCNDH ELMEQSGELR DINRHYYTLE 
           410        420        430        440        450
    EVEQDIQKPV VQRLLSLMKF RSNYPAFDGH FELNYSNNSS VAMAWRHGDY 
           460        470        480
    YCHLFVDLNF KTVKVTYTDV ETGETRHLEC
    Length:480
    Mass (Da):54,825
    Last modified:February 8, 2011 - 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:iDC990A3BD05E0C9E
    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
    		CP001978 Genomic DNA Translation: ADP98617.1

    NCBI Reference Sequences

    More...    RefSeqi    		WP_014578108.1, NC_017506.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		ADP98617; ADP98617; HP15_2853

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mad:HP15_2853

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|225937.3.peg.2880

    <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
    		CP001978 Genomic DNA Translation: ADP98617.1
    RefSeqiWP_014578108.1, NC_017506.1

    3D structure databases

    SMRiE4PMA5
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi225937.HP15_2853

    Protein family/group databases

    CAZyiGH13, Glycoside Hydrolase Family 13

    Genome annotation databases

    EnsemblBacteriaiADP98617; ADP98617; HP15_2853
    KEGGimad:HP15_2853
    PATRICifig|225937.3.peg.2880

    Phylogenomic databases

    eggNOGiCOG0366, Bacteria
    HOGENOMiCLU_021358_1_0_6
    OMAiCFMLEET

    Enzyme and pathway databases

    BioCyciMADH225937:G1GOU-2842-MONOMER
    MetaCyc:MONOMER-20515

    Family and domain databases

    CDDicd11355, AmyAc_Sucrose_phosphorylase, 1 hit
    InterProiView protein in InterPro
    IPR006047, Glyco_hydro_13_cat_dom
    IPR017853, Glycoside_hydrolase_SF
    IPR016377, Sucrose_GGa_phosphorylase-rel
    IPR022527, Sucrose_phospho
    PfamiView protein in Pfam
    PF00128, Alpha-amylase, 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 nameiGGOP_MARAH
    <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: E4PMA5
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 23, 2018
    Last sequence update: February 8, 2011
    Last modified: December 2, 2020
    This is version 58 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
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
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