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Entry version 108 (11 Dec 2019)
Sequence version 1 (01 Mar 2001)
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Protein

D-glyceraldehyde dehydrogenase (NADP(+))

Gene

Ta0809

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
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

NADP-dependent dehydrogenase of the nED (non-phosphorylated Entner-Doudoroff) pathway with highest activity towards glyceraldehydes (e.g. D,L-glyceraldehyde and D-glyceraldehyde), to a lesser extent towards D,L-glyceraldehyde-3-phosphate and glycolaldehyde, but no activity towards aliphatic or aromatic aldehydes.2 Publications

<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

Inhibited by calcium, cadmium, copper and mercury ions. Stable for 2 hours at 60 degrees Celsius but activity is decreased to less than 50 percent within 20 minutes at 80 degrees Celsius. Two folds activity enhancement in the presence of 1 mM glutathione, DTT, or 2-mercaptoethanol. Complete activity inhibition by thiol-modifying reagents such as p-chloromercuribenzoic acid or p-hydroxy-mercuribenzoic acid.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

kcat is 26 sec(-1) with glyceraldehyde as substrate, 20 sec(-1) with glyceraldehyde-3-phosphate as substrate, 37 sec(-1) with glycolaldehyde as substrate and 25 sec(-1) with NADP as substrate (at pH 7.9 and 58 degrees Celsius).1 Publication
  1. KM=0.2 mM for glyceraldehyde (at pH 7.9 and 58 degrees Celsius)1 Publication
  2. KM=18.3 mM for glyceraldehyde-3-phosphate (at pH 7.9 and 58 degrees Celsius)1 Publication
  3. KM=12.3 mM for glycolaldehyde (at pH 7.9 and 58 degrees Celsius)1 Publication
  4. KM=0.36 mM for NADP (at pH 7.9 and 58 degrees Celsius)1 Publication
  5. KM=0.33 mM for D,L-glyceraldehyde (at pH 8 and 50 degrees Celsius)1 Publication
  6. KM=0.017 mM for NADP (at pH 8 and 50 degrees Celsius)1 Publication
  1. Vmax=0.3 µmol/min/mg enzyme with D,L-glyceraldehyde as substrate (at pH 8 and 50 degrees Celsius)1 Publication
  2. Vmax=0.3 µmol/min/mg enzyme with NADP as substrate (at pH 8 and 50 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.6-8.2 Publications

Temperature dependencei

Optimum temperature is 50-55 degrees Celsius at pH 8 and 63 degrees Celsius at pH 7.6.2 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: glycolysis

This protein is involved in the pathway glycolysis, which is part of Carbohydrate degradation.1 Publication
View all proteins of this organism that are known to be involved in the pathway glycolysis and in Carbohydrate degradation.

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 sitei149SubstrateBy 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>Sitei149Transition state stabilizerBy similarity1
Binding sitei157NADPBy similarity1
Binding sitei157SubstrateBy 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 sitei247Proton acceptorPROSITE-ProRule annotation1
Active sitei281Proton donorBy similarity1
Binding sitei281NADPBy similarity1
Binding sitei281Substrate; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi146 – 149NADPBy similarity4
Nucleotide bindingi172 – 176NADPBy similarity5
Nucleotide bindingi204 – 210NADPBy similarity7
Nucleotide bindingi225 – 248NADPBy similarityAdd BLAST24
Nucleotide bindingi381 – 383NADPBy 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

  • glyceraldehyde dehydrogenase (NADP) activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

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 functionOxidoreductase
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
TACI273075:G1GT7-903-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.1.89 6324

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q9HK01

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

More...
UniPathwayi
UPA00109

<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:
D-glyceraldehyde dehydrogenase (NADP(+))1 Publication (EC:1.2.1.892 Publications)
Short name:
GADH1 Publication
Short name:
Glyceraldehyde DH1 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
Ordered Locus Names:Ta0809Imported
<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>OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)Imported
<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 identifieri273075 [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 lineageiArchaeaEuryarchaeotaDiaforarchaea groupThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
<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
  • UP000001024 <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

<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_00004307401 – 493D-glyceraldehyde dehydrogenase (NADP(+))Add BLAST493

<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

Homotetramer. Dimer of dimers.

2 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
273075.Ta0809

<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

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q9HK01

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

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili70 – 92Sequence analysisAdd BLAST23

<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 aldehyde dehydrogenase family. Glyceraldehyde dehydrogenase subfamily.UniRule annotationCurated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
arCOG01252 Archaea
COG1012 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000271509

KEGG Orthology (KO)

More...
KOi
K18128

Identification of Orthologs from Complete Genome Data

More...
OMAi
ERWSPAC

Database of Orthologous Groups

More...
OrthoDBi
56373at2157

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.309.10, 1 hit
3.40.605.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR016163 Ald_DH_C
IPR016160 Ald_DH_CS_CYS
IPR029510 Ald_DH_CS_GLU
IPR016162 Ald_DH_N
IPR015590 Aldehyde_DH_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00171 Aldedh, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53720 SSF53720, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 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.

Q9HK01-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDTKLYIDGQ WVNSSSGKTV DKYSPVTGQV IGRFEAATRD DVDRAIDAAE
60 70 80 90 100
DAFWAWNDLG SVERSKIIYR AKELIEKNRA ELENIIMEEN GKPVKEAKEE
110 120 130 140 150
VDGVIDQIQY YAEWARKLNG EVVEGTSSHR KIFQYKVPYG IVVALTPWNF
160 170 180 190 200
PAGMVARKLA PALLTGNTVV LKPSSDTPGS AEWIVRKFVE AGVPKGVLNF
210 220 230 240 250
ITGRGSEIGD YIVEHKKVNL ITMTGSTATG QRIMQKASAN MAKLILELGG
260 270 280 290 300
KAPFMVWKDA DMDNALKTLL WAKYWNAGQS CIAAERLYVH EDIYDTFMSR
310 320 330 340 350
FVELSRKLAL GDPKNADMGP LINKGALQAT SEIVEEAKES GAKILFGGSQ
360 370 380 390 400
PSLSGPYRNG YFFLPTIIGN ADQKSKIFQE EIFAPVIGAR KISSVEEMYD
410 420 430 440 450
LANDSKYGLA SYLFTKDPNI IFEASERIRF GELYVNMPGP EASQGYHTGF
460 470 480 490
RMTGQAGEGS KYGISEYLKL KNIYVDYSGK PLHINTVRDD LFQ
Length:493
Mass (Da):54,782
Last modified:March 1, 2001 - 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:i2F6A79DD96BE7FF5
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
AL445065 Genomic DNA Translation: CAC11938.1

NCBI Reference Sequences

More...
RefSeqi
WP_010901221.1, NC_002578.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAC11938; CAC11938; CAC11938

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1456354

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
tac:Ta0809

<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
AL445065 Genomic DNA Translation: CAC11938.1
RefSeqiWP_010901221.1, NC_002578.1

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
5IZDX-ray2.05A/B/C/D/E/F/G/H1-493[»]
5J77X-ray2.10A/B/C/D1-493[»]
5M4XX-ray3.56A/B/C/D1-493[»]
SMRiQ9HK01
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0809

Genome annotation databases

EnsemblBacteriaiCAC11938; CAC11938; CAC11938
GeneIDi1456354
KEGGitac:Ta0809

Phylogenomic databases

eggNOGiarCOG01252 Archaea
COG1012 LUCA
HOGENOMiHOG000271509
KOiK18128
OMAiERWSPAC
OrthoDBi56373at2157

Enzyme and pathway databases

UniPathwayiUPA00109
BioCyciTACI273075:G1GT7-903-MONOMER
BRENDAi1.2.1.89 6324
SABIO-RKiQ9HK01

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR016163 Ald_DH_C
IPR016160 Ald_DH_CS_CYS
IPR029510 Ald_DH_CS_GLU
IPR016162 Ald_DH_N
IPR015590 Aldehyde_DH_dom
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 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 nameiGADH_THEAC
<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: Q9HK01
<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: October 29, 2014
Last sequence update: March 1, 2001
Last modified: December 11, 2019
This is version 108 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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