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Entry version 36 (17 Jun 2020)
Sequence version 1 (09 Jan 2013)
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Protein

Glucosylglycerate hydrolase

Gene

ggh

Organism
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum)
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 hydrolysis of glucosylglycerate (GG) to glycerate and glucose (PubMed:25341489, PubMed:31316802). Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions (PubMed:25341489). Can also hydrolyze mannosylglycerate (MG), with tenfold lower efficiency (PubMed:31316802).2 Publications

<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 <a href="http://www.uniprot.org/help/function%5Fsection">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

Activity is not dependent on divalent cations, but it is enhanced by Mg2+.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

  1. KM=16.7 mM for glucosylglycerate (at 37 degrees Celsius, C-terminally tagged variant)1 Publication
  2. KM=16.7 mM for glucosylglycerate (at 42 degrees Celsius, C-terminally tagged variant)1 Publication
  3. KM=11.2 mM for glucosylglycerate (at 50 degrees Celsius, C-terminally tagged variant)1 Publication
  1. Vmax=13.7 µmol/min/mg enzyme with glucosylglycerate as substrate (at 37 degrees Celsius, C-terminally tagged variant)1 Publication
  2. Vmax=15.2 µmol/min/mg enzyme with glucosylglycerate as substrate (at 42 degrees Celsius, C-terminally tagged variant)1 Publication
  3. Vmax=12.3 µmol/min/mg enzyme with glucosylglycerate as substrate (at 50 degrees Celsius, C-terminally tagged variant)1 Publication
  4. Vmax=3.60 µmol/min/mg enzyme with glucosylglycerate as substrate (at 50 degrees Celsius, tag-less variant)1 Publication
  5. Vmax=3.09 µmol/min/mg enzyme with mannosylglycerate as substrate (at 50 degrees Celsius, tag-less variant)1 Publication

pH dependencei

Optimum pH is 6.0 (tag-less variant) (PubMed:31316802). Optimum pH is 5.8 (C-terminally tagged variant) (PubMed:25341489).2 Publications

Temperature dependencei

Optimum temperature is 50-55 degrees Celsius (tag-less variant) (PubMed:31316802). Optimum temperature is 42 degrees Celsius (C-terminally tagged variant) (PubMed:25341489).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei36Substrate1 Publication1
Binding sitei88Substrate1 Publication1
Binding sitei115Substrate1 Publication1
Binding sitei180Substrate; via carbonyl oxygen1 Publication1
<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 sitei182Proton donor1 Publication1
Binding sitei216Substrate1 Publication1
Active sitei419Proton acceptor1 Publication1
Binding sitei434Substrate1 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 functionGlycosidase, Hydrolase
Biological processStress response

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MHAS1122247:G11ND-2644-MONOMER

<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:
Glucosylglycerate hydrolase1 Publication (EC:3.2.1.2082 Publications)
Short name:
GG hydrolase1 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:ggh1 Publication
ORF Names:C731_0006Imported
<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>OrganismiMycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum)
<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 identifieri1122247 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
<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
  • UP000006265 <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: Unassembled WGS sequence

<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%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>Mutagenesisi43D → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi182D → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi419E → A: Loss of 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_00004499381 – 446Glucosylglycerate hydrolaseAdd BLAST446

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in response to nitrogen shock.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer. Dimer of dimers.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
1122247.C731_0006

<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
K5BDL0

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>Regioni40 – 43Substrate binding1 Publication4
Regioni375 – 376Substrate binding1 Publication2

<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 63 family.Curated

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
NSPRWDS

Database of Orthologous Groups

More...
OrthoDBi
70058at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR004888 Glycoside_hydrolase_63

The PANTHER Classification System

More...
PANTHERi
PTHR10412 PTHR10412, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48208 SSF48208, 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.

K5BDL0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPHDPSFTPT QLAARAAYLL RGNDLGTMTT AAPLLYPHMW SWDAAFVAIG
60 70 80 90 100
LAPLSVERAV VELDTLLSAQ WRNGMIPHIV FANGVDGYFP GPARWATATL
110 120 130 140 150
ADNAPRNRLT SGITQPPVHA IAVQRILEHA RTRGRSTRAV AEAFLDRRWG
160 170 180 190 200
DLMRWHRWLA ECRDRNERGR ITLYHGWESG MDNSPRWDSA YANVVPGKLP
210 220 230 240 250
EYQRADNVII TDPSQRPSDG EYDRYLWLLE EMKAVRYDDE RLPSVMSFQV
260 270 280 290 300
EDVFFSAIFS VACQVLAEIG EDYKRPHADV KDLYLWAERF RAGVVETTDQ
310 320 330 340 350
RTGAARDFDV LAEKWLVTET AAQFAPLLCG GLPHDRERAL LKLLEGPRFC
360 370 380 390 400
GHPDLKYGLI PSTSPVSRDF RPREYWRGPV WPVLTWLFSW CFARRGWAER
410 420 430 440
ARLLRQEGLR QASDGSFAEY YEPFTGEPLG SMQQSWTAAA VLDWLG
Length:446
Mass (Da):50,769
Last modified:January 9, 2013 - 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:iE7856A89CE5665AB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AMRA01000001 Genomic DNA Translation: EKF25940.1

NCBI Reference Sequences

More...
RefSeqi
WP_005623031.1, NZ_LR026975.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
EKF25940; EKF25940; C731_0006

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1122247.3.peg.6

<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
AMRA01000001 Genomic DNA Translation: EKF25940.1
RefSeqiWP_005623031.1, NZ_LR026975.1

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
5OHCX-ray2.00A/B1-446[»]
5OHZX-ray2.04A/B/C/D1-446[»]
5OI0X-ray1.68A/B1-446[»]
5OI1X-ray1.75A/B1-446[»]
5OIEX-ray2.07A/B1-446[»]
5OIVX-ray1.78A/B1-446[»]
5OIWX-ray1.71A/B1-446[»]
5OJ4X-ray1.79A/B1-446[»]
5OJUX-ray2.17A/B1-446[»]
5OJVX-ray2.06A/B1-446[»]
5ONTX-ray2.05A/B1-446[»]
5ONZX-ray1.93A/B1-446[»]
5OO2X-ray2.06A/B1-446[»]
6G3NX-ray2.32A/B1-446[»]
6Q5TX-ray2.54A/B1-446[»]
SMRiK5BDL0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi1122247.C731_0006

Genome annotation databases

EnsemblBacteriaiEKF25940; EKF25940; C731_0006
PATRICifig|1122247.3.peg.6

Phylogenomic databases

OMAiNSPRWDS
OrthoDBi70058at2

Enzyme and pathway databases

BioCyciMHAS1122247:G11ND-2644-MONOMER

Family and domain databases

Gene3Di1.50.10.10, 1 hit
InterProiView protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR004888 Glycoside_hydrolase_63
PANTHERiPTHR10412 PTHR10412, 2 hits
SUPFAMiSSF48208 SSF48208, 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 nameiGGH_MYCHD
<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: K5BDL0
<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: June 17, 2020
Last sequence update: January 9, 2013
Last modified: June 17, 2020
This is version 36 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, 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
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