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Protein

Trehalose synthase/amylase TreS

Gene

treS

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
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 interconversion of maltose and trehalose by transglucosylation (PubMed:15511231, PubMed:18505459, PubMed:20118231, PubMed:21840994). Maltose is the preferred substrate (PubMed:15511231, PubMed:18505459). To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose (PubMed:18505459). TreS plays a key role in the utilization of trehalose for the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P) (PubMed:20118231, PubMed:27513637). Might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.5 Publications

Miscellaneous

Maltose-1-phosphate (M1P), the building block required for alpha-glucan production, is generated by two alternative routes: the TreS-Pep2 branch and the GlgC-GlgM branch, however it seems that the GlgC-GlgM branch provides most of M1P for the GlgE pathway in M.smegmatis.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section 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

The amylase activity is stimulated by addition of Ca2+, but this cation and other divalent cations inhibit the trehalose synthase activity. In addition, trehalose synthase activity, but not amylase activity, is strongly inhibited, and in a competitive manner, by validoxylamine. On the other hand, amylase, but not trehalose synthase activity, is inhibited by the known transition-state amylase inhibitor, acarbose, suggesting the possibility of two different active sites. Other metal ions such as Mg2+, Mn2+, and Co2+ are also somewhat effective in the stimulation of amylase activity, but Hg2+, Cu2+, Ni2+ and Zn2+ are inhibitory.3 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=8.0 mM for maltose (at pH 6.8 and 37 degrees Celsius)3 Publications
  2. KM=87 mM for trehalose (at pH 6.8 and at 37 degrees Celsius)3 Publications
  3. KM=2.9 mM for 2,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  4. KM=2.5 mM for 3,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  5. KM=2.2 mM for 4-chloro-2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  6. KM=5.8 mM for 4-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  7. KM=0.7 mM for 2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)3 Publications
  8. KM=0.15 mM for alpha-glucosyl fluoride (at pH 6.8 and 37 degrees Celsius)3 Publications

    pH dependencei

    Optimum pH is between 6.0-6.2 for the amylase activity and 7.0 for the trehalose synthase activity.2 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycogen biosynthesis

    This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.2 Publications
    View all proteins of this organism that are known to be involved in the pathway glycogen biosynthesis and in Glycan biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei90SubstrateBy similarity1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi132CalciumCombined sources1 Publication1
    Binding sitei133SubstrateBy similarity1
    Binding sitei198SubstrateBy similarity1
    Metal bindingi200CalciumCombined sources1 Publication1
    Binding sitei228SubstrateBy similarity1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei230Nucleophile1 Publication1
    Metal bindingi234Calcium; via carbonyl oxygenCombined sources1 Publication1
    Metal bindingi235Calcium; via carbonyl oxygenCombined sources1 Publication1
    Metal bindingi237CalciumCombined sources1 Publication1
    Active sitei272Proton donorBy similarity1
    Binding sitei341SubstrateBy similarity1
    Binding sitei342SubstrateBy similarity1

    <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, Isomerase
    Biological processCarbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism, Polysaccharide degradation
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-6023
    MSME246196:G1H7P-6481-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    5.4.99.16 3512

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

    More...
    UniPathwayi
    UPA00164

    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:
    Trehalose synthase/amylase TreS1 Publication (EC:3.2.1.11 Publication, EC:5.4.99.163 Publications)
    Alternative name(s):
    Maltose alpha-D-glucosyltransferase1 Publication
    Short name:
    MTase1 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:treS1 Publication
    Ordered Locus Names:MSMEG_6515, MSMEI_6343
    <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>OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    <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 identifieri246196 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
    <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
    • UP000006158 <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
    • UP000000757 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 in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene do not accumulate increased amounts of glycogen in the presence of trehalose and show only a small effect in alpha-glucan (PubMed:20118231, PubMed:27513637). Combined inactivation of treS with glgB or glgC completely blocks alpha-glucan production (PubMed:27513637).2 Publications

    <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_00004129051 – 593Trehalose synthase/amylase TreSAdd BLAST593

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    A0R6E0

    <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

    Homohexamer.1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    246196.MSMEG_6515

    <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

    1593
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    A0R6E0

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

    More...
    SMRi
    A0R6E0

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CG3 Bacteria
    COG0366 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000220639

    KEGG Orthology (KO)

    More...
    KOi
    K05343

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    PNGEKWA

    Database of Orthologous Groups

    More...
    OrthoDBi
    POG091H07NZ

    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
    IPR006047 Glyco_hydro_13_cat_dom
    IPR013780 Glyco_hydro_b
    IPR017853 Glycoside_hydrolase_SF
    IPR032091 Malt_amylase_C
    IPR012810 TreS/a-amylase_N

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00128 Alpha-amylase, 1 hit
    PF16657 Malt_amylase_C, 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
    TIGR02456 treS_nterm, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    A0R6E0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEEHTQGSHV EAGIVEHPNA EDFGHARTLP TDTNWFKHAV FYEVLVRAFY
    60 70 80 90 100
    DSNADGIGDL RGLTEKLDYI KWLGVDCLWL PPFYDSPLRD GGYDIRDFYK
    110 120 130 140 150
    VLPEFGTVDD FVTLLDAAHR RGIRIITDLV MNHTSDQHEW FQESRHNPDG
    160 170 180 190 200
    PYGDFYVWSD TSDRYPDARI IFVDTEESNW TFDPVRRQFY WHRFFSHQPD
    210 220 230 240 250
    LNYDNPAVQE AMLDVLRFWL DLGIDGFRLD AVPYLFEREG TNCENLPETH
    260 270 280 290 300
    AFLKRCRKAI DDEYPGRVLL AEANQWPADV VAYFGDPDTG GDECHMAFHF
    310 320 330 340 350
    PLMPRIFMAV RRESRFPISE ILAQTPPIPD TAQWGIFLRN HDELTLEMVT
    360 370 380 390 400
    DEERDYMYAE YAKDPRMKAN VGIRRRLAPL LENDRNQIEL FTALLLSLPG
    410 420 430 440 450
    SPVLYYGDEI GMGDIIWLGD RDSVRTPMQW TPDRNAGFSK ATPGRLYLPP
    460 470 480 490 500
    NQDAVYGYHS VNVEAQLDSS SSLLNWTRNM LAVRSRHDAF AVGTFRELGG
    510 520 530 540 550
    SNPSVLAYIR EVTRQQGDGG AKTDAVLCVN NLSRFPQPIE LNLQQWAGYI
    560 570 580 590
    PVEMTGYVEF PSIGQLPYLL TLPGHGFYWF QLREPDPEPG AQQ
    Length:593
    Mass (Da):68,201
    Last modified:January 9, 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:iD63935658A86B6E4
    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
    CP000480 Genomic DNA Translation: ABK71531.1
    CP001663 Genomic DNA Translation: AFP42769.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_003897929.1, NZ_CP009494.1
    YP_890728.1, NC_008596.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ABK71531; ABK71531; MSMEG_6515
    AFP42769; AFP42769; MSMEI_6343

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    4533171

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    msb:LJ00_32205
    msg:MSMEI_6343
    msm:MSMEG_6515

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|246196.19.peg.6339

    <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
    CP000480 Genomic DNA Translation: ABK71531.1
    CP001663 Genomic DNA Translation: AFP42769.1
    RefSeqiWP_003897929.1, NZ_CP009494.1
    YP_890728.1, NC_008596.1

    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
    3ZO9X-ray1.84A/B1-593[»]
    3ZOAX-ray1.85A/B1-593[»]
    5JY7X-ray3.60A/B/C/D/E/F/G/H1-593[»]
    ProteinModelPortaliA0R6E0
    SMRiA0R6E0
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi246196.MSMEG_6515

    Protein family/group databases

    CAZyiGH13 Glycoside Hydrolase Family 13

    Proteomic databases

    PRIDEiA0R6E0

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABK71531; ABK71531; MSMEG_6515
    AFP42769; AFP42769; MSMEI_6343
    GeneIDi4533171
    KEGGimsb:LJ00_32205
    msg:MSMEI_6343
    msm:MSMEG_6515
    PATRICifig|246196.19.peg.6339

    Phylogenomic databases

    eggNOGiENOG4105CG3 Bacteria
    COG0366 LUCA
    HOGENOMiHOG000220639
    KOiK05343
    OMAiPNGEKWA
    OrthoDBiPOG091H07NZ

    Enzyme and pathway databases

    UniPathwayi
    UPA00164

    BioCyciMetaCyc:MONOMER-6023
    MSME246196:G1H7P-6481-MONOMER
    BRENDAi5.4.99.16 3512

    Family and domain databases

    Gene3Di2.60.40.1180, 1 hit
    InterProiView protein in InterPro
    IPR006047 Glyco_hydro_13_cat_dom
    IPR013780 Glyco_hydro_b
    IPR017853 Glycoside_hydrolase_SF
    IPR032091 Malt_amylase_C
    IPR012810 TreS/a-amylase_N
    PfamiView protein in Pfam
    PF00128 Alpha-amylase, 1 hit
    PF16657 Malt_amylase_C, 1 hit
    SMARTiView protein in SMART
    SM00642 Aamy, 1 hit
    SUPFAMiSSF51445 SSF51445, 1 hit
    TIGRFAMsiTIGR02456 treS_nterm, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTRES_MYCS2
    <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: A0R6E0
    Secondary accession number(s): I7GGI2
    <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: September 21, 2011
    Last sequence update: January 9, 2007
    Last modified: December 5, 2018
    This is version 83 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    UniProt is an ELIXIR core data resource
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