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UniProtKB - Q6L047 (GLCD2_PICTO)

Entry version 103 (23 Feb 2022)
Sequence version 1 (05 Jul 2004)
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Protein

Glucose/galactose 1-dehydrogenase

Gene

gdh2

Organism
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
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 NAD(P)+-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Is also significantly active with D-galactose as substrate, but not with D-xylose, L-arabinose, D-ribose, D-mannose, D-allose, D-glucosamine, 2-deoxy-D-glucose, or glucose-6-phosphate. Can utilize both NAD+ and NADP+ as electron acceptor, with a marked preference for NADP+ (20-fold higher activity). Physiologically, may be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway.

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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarityNote: Zn2+ is of critical importance for the stability of the enzyme.By similarity

<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=10 mM for D-glucose1 Publication
  2. KM=4.5 mM for D-galactose1 Publication
  3. KM=1.12 mM for NADP+1 Publication

pH dependencei

Optimum pH is 6.5 for the oxidation of D-glucose by NADP+. At the physiological pH of 4.6 found in the cytoplasm of Picrophilus cells, the enzyme shows merely 10% of its maximal activity.1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius for the oxidation of D-glucose by NADP+.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 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 bindingi39Zinc; catalyticBy 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 sitei41SubstrateBy similarity1
Metal bindingi66Zinc; via tele nitrogen; catalyticBy similarity1
Metal bindingi67Zinc; catalyticBy similarity1
Binding sitei116SubstrateBy similarity1
Metal bindingi153Zinc; catalyticBy similarity1
Binding sitei153SubstrateBy similarity1
Binding sitei157SubstrateBy similarity1
Binding sitei304SubstrateBy similarity1
Binding sitei347NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi213 – 215NADPBy similarity3
Nucleotide bindingi273 – 275NADPBy similarity3
Nucleotide bindingi302 – 304NADPBy similarity3

<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 functionOxidoreductase
Biological processCarbohydrate metabolism
LigandMetal-binding, NAD, NADP, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.360, 7518

<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:
Glucose/galactose 1-dehydrogenase (EC:1.1.1.360)
Alternative name(s):
Galactose 1-dehydrogenase [NADP(+)]
Glucose 1-dehydrogenase 2
Short name:
GDH 2
Short name:
GlcDH 2
<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:gdh2
Synonyms:gdhA
Ordered Locus Names:PTO1070
<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>OrganismiPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
<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 identifieri263820 [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 lineageiArchaea › Candidatus Thermoplasmatota › Thermoplasmata › Thermoplasmatales › Picrophilaceae › Picrophilus ›
<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
  • UP000000438 <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 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_00004148371 – 359Glucose/galactose 1-dehydrogenaseAdd BLAST359

<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.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		263820.PTO1070

<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		Q6L047

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 zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		arCOG01459, Archaea

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_026673_1_0_2

Identification of Orthologs from Complete Genome Data

More...OMAi		MCRNGRY

Database of Orthologous Groups

More...OrthoDBi		43162at2157

Family and domain databases

HAMAP database of protein families

More...HAMAPi		MF_02127, Glucose_DH, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013154, ADH_N
IPR026583, Glc_1-DH_arc
IPR031640, Glu_dehyd_C
IPR011032, GroES-like_sf
IPR036291, NAD(P)-bd_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08240, ADH_N, 1 hit
PF16912, Glu_dehyd_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 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.

Q6L047-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVRAIITNAP NGGVKIENVN INEPEHYEVK LRPVYTGLCG TDRGEVLGNL 
        60         70         80         90        100
SFAYNEPGYN YLVLGHEAIC QVIEASENPY KIKPGDYVVP VVRRPGKCVN 
       110        120        130        140        150
CRIGREDDCS DGDKHEAGIT GLHGFMRDYF YDEAKNLVKI NDKNMVKVAV 
       160        170        180        190        200
LTEPTKNVMK AFEVFDTVSK RSIFQGDDST NLTKNCLIIG TGSEAFLYAF 
       210        220        230        240        250
MAREYRFNVF MTNRHPVGEE KLSIISRINA DFYDYTREDP LKGIDLLIDT 
       260        270        280        290        300
SGDPGTIFRF VRKMNYNGVV ILFGTNGRAP ATSIDGEDID YIIERNISLV 
       310        320        330        340        350
GSVDGAKRHY LRAVEYLEKW NYSEGSVINR LITGVFEPED VSIFTKKPEN 

EIKSVIKWS
Length:359
Mass (Da):40,463
Last modified:July 5, 2004 - 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:i7CAC2E1480E4B7C7
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
AE017261 Genomic DNA Translation: AAT43655.1

NCBI Reference Sequences

More...RefSeqi		WP_011177871.1, NC_005877.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAT43655; AAT43655; PTO1070

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2844646

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		pto:PTO1070

<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
AE017261 Genomic DNA Translation: AAT43655.1
RefSeqiWP_011177871.1, NC_005877.1

3D structure databases

SMRiQ6L047
ModBaseiSearch...

Protein-protein interaction databases

STRINGi263820.PTO1070

Genome annotation databases

EnsemblBacteriaiAAT43655; AAT43655; PTO1070
GeneIDi2844646
KEGGipto:PTO1070

Phylogenomic databases

eggNOGiarCOG01459, Archaea
HOGENOMiCLU_026673_1_0_2
OMAiMCRNGRY
OrthoDBi43162at2157

Enzyme and pathway databases

BRENDAi1.1.1.360, 7518

Family and domain databases

HAMAPiMF_02127, Glucose_DH, 1 hit
InterProiView protein in InterPro
IPR013154, ADH_N
IPR026583, Glc_1-DH_arc
IPR031640, Glu_dehyd_C
IPR011032, GroES-like_sf
IPR036291, NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF08240, ADH_N, 1 hit
PF16912, Glu_dehyd_C, 1 hit
SUPFAMiSSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 1 hit

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 nameiGLCD2_PICTO
<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: Q6L047
<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: January 25, 2012
Last sequence update: July 5, 2004
Last modified: February 23, 2022
This is version 103 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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