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Entry version 110 (08 May 2019)
Sequence version 1 (01 May 2000)
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Protein

Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

Gene

glgE

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

Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is also able to catalyze the reverse reaction in vitro. Cannot use glucose 1-phosphate as substrate. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.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 <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

The transfer reaction from maltose-1-P to glycogen is inhibited by micromolar amounts of inorganic phosphate or arsenate but is only slightly inhibited by millimolar concentrations of glucose-1-P, glucose-6-P, or inorganic pyrophosphate. Is also inhibited by ATP, by 1,4-dideoxy-1,4-imino-D-arabinitol (DIA), but not by isofagomine.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

The data are not very reliable because measures were done with a partially purified enzyme.
  1. KM=250 µM for maltose 1-phosphate1 Publication
  1. Vmax=25.2 nmol/min/mg enzyme1 Publication

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

This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.1 Publication
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 <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 sitei284Maltose 1-phosphateBy similarity1
Binding sitei344Maltose 1-phosphateBy similarity1
Binding sitei379Maltose 1-phosphateBy similarity1
<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 sitei414NucleophileBy similarity1
Binding sitei415Maltose 1-phosphateBy similarity1
Active sitei443Proton donorBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei499Transition state stabilizerBy 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 functionGlycosyltransferase, Transferase
Biological processCarbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.99.16 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:
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (EC:2.4.99.16)
Short name:
GMPMT
Alternative name(s):
(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase
<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:glgE
Ordered Locus Names:MSMEG_4916, MSMEI_4789
<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 display M1P accumulation and trehalose sensitivity. These phenotypes are suppressed in mutants lacking both glgE and treS or both glgE and mak. Deletion of glgE does not increase glycogen content.1 Publication

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>Mutagenesisi349H → Y in SMEG53; results in a temperature-dependent accumulation of M1P during exponential growth. 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_00000543461 – 697Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferaseAdd BLAST697

<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.1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
246196.MSMEI_4789

<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
Q9RP48

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

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>Regioni553 – 554Maltose 1-phosphate bindingBy similarity2

<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
ENOG4105EP6 Bacteria
COG0366 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000239230

KEGG Orthology (KO)

More...
KOi
K16147

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit
2.60.40.1180, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_02124 GlgE, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR026585 GlgE
IPR021828 GlgE_dom_N/S
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF11896 DUF3416, 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

<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.

Q9RP48-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRSGWVAGRI GIDDVAPVVS CGRYPAKAVV GEVVPVRATV WREGHDAVSA
60 70 80 90 100
TLVVRYLGTE FPRLASGPGT TPPAVPLGTV VQPGKRVKPQ ILQMSKGRTP
110 120 130 140 150
DVFHGEFTPD AVGLWTFRVD GWGDPIATWR HAVEAKLEAG QSETELNNDL
160 170 180 190 200
LVGARLLMRA AEGVPRKLRD PLLEAAQQLR TPGDPYQRAG GALSPEVADL
210 220 230 240 250
LLQYPLREFV TRGEVHGVWV DRPLARFSSW YEMFPRSTGG WDENGHPVHG
260 270 280 290 300
TFATAAAALP RIARMGFNVV YLPPIHPIGK VHRKGRNNSV TAAPGDVGSP
310 320 330 340 350
WAIGSDEGGH DAVHPDLGTI DDFDAFVAAA RDAGLEVALD LALQCAPDHP
360 370 380 390 400
WAKEHPEWFT VLPDGTIAYA ENPPKKYQDI YPLNFDNDPD GLFHEVLRVV
410 420 430 440 450
KFWISHGVKV FRVDNPHTKP PNFWAWLIAE VKNEDPDILF LSEAFTRPAR
460 470 480 490 500
LYGLAKLGFT QSYTYFTWRT AKWELTEFGE EIAKYADHAR PNLWVNTPDI
510 520 530 540 550
LHESLQHGGP GMFAIRAVLA STMSSSWGVY SGYELFEHRS VREGSEEYLD
560 570 580 590 600
SEKYELRPRD FDGALARGES LEPFLTRLNE IRRLHPALRQ LRTIKFHHLD
610 620 630 640 650
NDALLAYSKF DPVTGDTVLV VVTLNPFGPE ESTLWLDMEA LGMEPYDRFW
660 670 680 690
VRDEITGEEY QWGQSNYVRI EPAKAVAHVL NMPLIPYEKR LDLLRRE
Length:697
Mass (Da):78,043
Last modified:May 1, 2000 - 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:iE1B92754318A1E55
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence ABK71468 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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
AF172946 Genomic DNA Translation: AAF07898.1
CP000480 Genomic DNA Translation: ABK71468.1 Different initiation.
CP001663 Genomic DNA Translation: AFP41237.1

NCBI Reference Sequences

More...
RefSeqi
YP_889171.1, NC_008596.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABK71468; ABK71468; MSMEG_4916
AFP41237; AFP41237; MSMEI_4789

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4532624

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
msg:MSMEI_4789
msm:MSMEG_4916

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|246196.19.peg.4797

<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
AF172946 Genomic DNA Translation: AAF07898.1
CP000480 Genomic DNA Translation: ABK71468.1 Different initiation.
CP001663 Genomic DNA Translation: AFP41237.1
RefSeqiYP_889171.1, NC_008596.1

3D structure databases

SMRiQ9RP48
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEI_4789

Protein family/group databases

CAZyiGH13 Glycoside Hydrolase Family 13

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK71468; ABK71468; MSMEG_4916
AFP41237; AFP41237; MSMEI_4789
GeneIDi4532624
KEGGimsg:MSMEI_4789
msm:MSMEG_4916
PATRICifig|246196.19.peg.4797

Phylogenomic databases

eggNOGiENOG4105EP6 Bacteria
COG0366 LUCA
HOGENOMiHOG000239230
KOiK16147

Enzyme and pathway databases

UniPathwayiUPA00164
BRENDAi2.4.99.16 3512

Family and domain databases

Gene3Di2.60.40.10, 1 hit
2.60.40.1180, 1 hit
HAMAPiMF_02124 GlgE, 1 hit
InterProiView protein in InterPro
IPR026585 GlgE
IPR021828 GlgE_dom_N/S
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF11896 DUF3416, 1 hit
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SUPFAMiSSF51445 SSF51445, 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 nameiGLGE_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: Q9RP48
Secondary accession number(s): A0R1Y3, I7G6B6
<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 3, 2003
Last sequence update: May 1, 2000
Last modified: May 8, 2019
This is version 110 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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