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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

DLD

Organism
Homo sapiens (Human)
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

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).By similarity7 Publications

Miscellaneous

The active site is a redox-active disulfide bond.By similarity

<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 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

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

<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

Disruption of native heterodimer state inhibits primary dihydrolipoamide dehydrogenase activity and induces serine protease activity.1 Publication

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 sitei89FAD1 Publication1
Binding sitei154FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei243NAD1 Publication1
Binding sitei278NAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei314NAD; via amide nitrogen1 Publication1
Binding sitei355FAD1 Publication1
<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>Sitei448Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex1 Publication1
Sitei473Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex1 Publication1
<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 sitei487Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi71 – 80FAD1 Publication10
Nucleotide bindingi183 – 185FAD1 Publication3
Nucleotide bindingi220 – 227NAD1 Publication8
Nucleotide bindingi361 – 364FAD1 Publication4

<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 functionOxidoreductase
LigandFAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS01727-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.8.1.4 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-HSA-389661 Glyoxylate metabolism and glycine degradation
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-6783984 Glycine degradation
R-HSA-70268 Pyruvate metabolism
R-HSA-70895 Branched-chain amino acid catabolism
R-HSA-71064 Lysine catabolism
R-HSA-71403 Citric acid cycle (TCA cycle)

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P09622

<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:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.46 Publications)
Alternative name(s):
Dihydrolipoamide dehydrogenase
Glycine cleavage system L protein
<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:DLD
Synonyms:GCSL, LAD, PHE3
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000091140.12

Human Gene Nomenclature Database

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HGNCi
HGNC:2898 DLD

Online Mendelian Inheritance in Man (OMIM)

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MIMi
238331 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P09622

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasmic vesicle, Flagellum, Mitochondrion, Nucleus

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Dihydrolipoamide dehydrogenase deficiency (DLDD)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive metabolic disorder characterized biochemically by a combined deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate dehydrogenase complex (KGDC). Clinically, affected individuals have lactic acidosis and neurologic deterioration due to sensitivity of the central nervous system to defects in oxidative metabolism.
See also OMIM:246900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07698547I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs397514651EnsemblClinVar.1
Natural variantiVAR_00690772K → E in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964987EnsemblClinVar.1
Natural variantiVAR_076986136Missing in DLDD. 1 Publication1
Natural variantiVAR_015820229G → C in DLDD. 2 PublicationsCorresponds to variant dbSNP:rs121964990EnsemblClinVar.1
Natural variantiVAR_076987361M → V in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964993EnsemblClinVar.1
Natural variantiVAR_076988375E → K in DLDD; loss of enzyme activity; abolished interaction with PDHX. 4 PublicationsCorresponds to variant dbSNP:rs121964992EnsemblClinVar.1
Natural variantiVAR_076989393I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964991EnsemblClinVar.1
Natural variantiVAR_076990479D → V in DLDD; reduced dehydrogenase activity; increased proteolytic activity. 2 PublicationsCorresponds to variant dbSNP:rs397514649EnsemblClinVar.1
Natural variantiVAR_076991482R → G in DLDD; reduced enzyme activity. Corresponds to variant dbSNP:rs397514650EnsemblClinVar.1
Natural variantiVAR_006908488P → L in DLDD; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964988EnsemblClinVar.1
Natural variantiVAR_015821495R → G in DLDD; loss of enzyme activity; reduced interaction with PDHX. 3 PublicationsCorresponds to variant dbSNP:rs121964989EnsemblClinVar.1

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>Mutagenesisi89K → E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. 1 Publication1
Mutagenesisi383H → A: Reduces dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi383H → L: Reduces dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi448D → A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi448D → N: Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi466E → A: Decreases dehydrogenase activity. Loss of proteolytic activity. 1 Publication1
Mutagenesisi473Y → A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi473Y → F: Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi473Y → H: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi482R → A: Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi482R → M: Does not affect interaction with PDHX. 1 Publication1
Mutagenesisi485H → A: Loss of dehydrogenase activity. Increases proteolytic activity. 1 Publication1
Mutagenesisi491S → A: Loss of proteolytic activity. Does not affect dehydrogenase activity. 1 Publication1
Mutagenesisi492E → Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. 1 Publication1
Mutagenesisi505K → M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
1738

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
DLD

MalaCards human disease database

More...
MalaCardsi
DLD
MIMi246900 phenotype

Open Targets

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OpenTargetsi
ENSG00000091140

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2394 Pyruvate dehydrogenase E3 deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27352

Chemistry databases

Drug and drug target database

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DrugBanki
DB03147 Flavin adenine dinucleotide
DB00157 NADH

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DLD

Domain mapping of disease mutations (DMDM)

More...
DMDMi
269849557

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 35MitochondrionCombined sourcesAdd BLAST35
<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_000003029536 – 509Dihydrolipoyl dehydrogenase, mitochondrialAdd BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei66N6-acetyllysine; alternateBy similarity1
Modified residuei66N6-succinyllysine; alternateBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi80 ↔ 85Redox-activeBy similarity
Modified residuei104N6-acetyllysine; alternateBy similarity1
Modified residuei104N6-succinyllysine; alternateBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-succinyllysine; alternateBy similarity1
Modified residuei132N6-acetyllysine; alternateBy similarity1
Modified residuei132N6-succinyllysine; alternateBy similarity1
Modified residuei143N6-acetyllysine; alternateCombined sources1
Modified residuei143N6-succinyllysine; alternateBy similarity1
Modified residuei159N6-succinyllysineBy similarity1
Modified residuei166N6-succinyllysineBy similarity1
Modified residuei273N6-succinyllysineBy similarity1
Modified residuei277N6-succinyllysineBy similarity1
Modified residuei285PhosphoserineBy similarity1
Modified residuei297PhosphoserineBy similarity1
Modified residuei346N6-acetyllysineBy similarity1
Modified residuei410N6-acetyllysine; alternateCombined sources1
Modified residuei410N6-succinyllysine; alternateBy similarity1
Modified residuei417N6-acetyllysineCombined sources1
Modified residuei420N6-acetyllysineBy similarity1
Modified residuei430N6-succinyllysineBy similarity1
Modified residuei502PhosphoserineCombined sources1
Modified residuei505N6-acetyllysine; alternateBy similarity1
Modified residuei505N6-succinyllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P09622

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P09622

MaxQB - The MaxQuant DataBase

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MaxQBi
P09622

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P09622

PeptideAtlas

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PeptideAtlasi
P09622

PRoteomics IDEntifications database

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PRIDEi
P09622

ProteomicsDB human proteome resource

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ProteomicsDBi
52254

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00015911

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P09622

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P09622

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P09622

SwissPalm database of S-palmitoylation events

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SwissPalmi
P09622

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000091140 Expressed in 234 organ(s), highest expression level in heart right ventricle

CleanEx database of gene expression profiles

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CleanExi
HS_DLD

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P09622 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P09622 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA044849

<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 (PubMed:15946682). Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDHA (PDHA1 or PDHA2) and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (PubMed:14638692). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (by non covalent bonds) (PubMed:14638692, PubMed:20361979). The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A (PubMed:29211711). Interacts with PDHX (PubMed:20385101, PubMed:16442803, PubMed:20160912, PubMed:20361979).7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108082, 375 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P09622

Database of interacting proteins

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DIPi
DIP-29027N

Protein interaction database and analysis system

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IntActi
P09622, 320 interactors

Molecular INTeraction database

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MINTi
P09622

STRING: functional protein association networks

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STRINGi
9606.ENSP00000205402

<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

1509
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZMCX-ray2.53A/B/C/D/E/F/G/H36-509[»]
1ZMDX-ray2.08A/B/C/D/E/F/G/H36-509[»]
1ZY8X-ray2.59A/B/C/D/E/F/G/H/I/J36-509[»]
2F5ZX-ray2.18A/B/C/D/E/F/G/H/I/J36-509[»]
3RNMX-ray2.40A/B/C/D36-509[»]
5J5ZX-ray1.84A/B36-509[»]
5NHGX-ray2.27A/B/C/D/E/F/G/H36-509[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P09622

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

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SMRi
P09622

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P09622

<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

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1335 Eukaryota
COG1249 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00550000074844

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000276708

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG002290

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P09622

KEGG Orthology (KO)

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KOi
K00382

Identification of Orthologs from Complete Genome Data

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OMAi
TMSEAVM

Database of Orthologous Groups

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OrthoDBi
581771at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P09622

TreeFam database of animal gene trees

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TreeFami
TF300414

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.390.30, 1 hit
3.50.50.60, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006258 Lipoamide_DH
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000350 Mercury_reductase_MerA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01350 lipoamide_DH, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 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>Sequences (3+)i

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P09622-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MQSWSRVYCS LAKRGHFNRI SHGLQGLSAV PLRTYADQPI DADVTVIGSG
60 70 80 90 100
PGGYVAAIKA AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM
110 120 130 140 150
AHGKDFASRG IEMSEVRLNL DKMMEQKSTA VKALTGGIAH LFKQNKVVHV
160 170 180 190 200
NGYGKITGKN QVTATKADGG TQVIDTKNIL IATGSEVTPF PGITIDEDTI
210 220 230 240 250
VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG
260 270 280 290 300
VGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK
310 320 330 340 350
AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQTKIPNI
360 370 380 390 400
YAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA
410 420 430 440 450
WVGKSEEQLK EEGIEYKVGK FPFAANSRAK TNADTDGMVK ILGQKSTDRV
460 470 480 490 500
LGAHILGPGA GEMVNEAALA LEYGASCEDI ARVCHAHPTL SEAFREANLA

ASFGKSINF
Length:509
Mass (Da):54,177
Last modified:November 24, 2009 - v2
<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:i7613492C516F3835
GO
Isoform 2 (identifier: P09622-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.

Note: No experimental confirmation available.
Show »
Length:410
Mass (Da):43,587
Checksum:i4FB4B37B7A801353
GO
Isoform 3 (identifier: P09622-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-194: Missing.

Note: No experimental confirmation available.
Show »
Length:461
Mass (Da):49,283
Checksum:iE9BB766499627F76
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PEX6E9PEX6_HUMAN
Dihydrolipoyl dehydrogenase
DLD
486Annotation score:

Annotation score:2 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>
F2Z2E3F2Z2E3_HUMAN
Dihydrolipoyl dehydrogenase, mitoch...
DLD
115Annotation score:

Annotation score:1 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>
F8WDM5F8WDM5_HUMAN
Dihydrolipoyl dehydrogenase, mitoch...
DLD
114Annotation score:

Annotation score:1 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>
A0A1W2PR83A0A1W2PR83_HUMAN
Dihydrolipoyl dehydrogenase, mitoch...
DLD
114Annotation score:

Annotation score:1 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>
F8WDY5F8WDY5_HUMAN
Dihydrolipoyl dehydrogenase, mitoch...
DLD
58Annotation score:

Annotation score:1 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>

<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 BAD92940 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti154G → R in AAA35764 (PubMed:3278312).Curated1
Sequence conflicti209L → F in BAD92940 (Ref. 5) Curated1
Sequence conflicti493A → AEA in AAB01381 (PubMed:8406489).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07698547I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs397514651EnsemblClinVar.1
Natural variantiVAR_00690772K → E in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964987EnsemblClinVar.1
Natural variantiVAR_031922104K → T2 PublicationsCorresponds to variant dbSNP:rs1130477Ensembl.1
Natural variantiVAR_076986136Missing in DLDD. 1 Publication1
Natural variantiVAR_015820229G → C in DLDD. 2 PublicationsCorresponds to variant dbSNP:rs121964990EnsemblClinVar.1
Natural variantiVAR_014555331L → V. Corresponds to variant dbSNP:rs17624Ensembl.1
Natural variantiVAR_076987361M → V in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964993EnsemblClinVar.1
Natural variantiVAR_076988375E → K in DLDD; loss of enzyme activity; abolished interaction with PDHX. 4 PublicationsCorresponds to variant dbSNP:rs121964992EnsemblClinVar.1
Natural variantiVAR_076989393I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964991EnsemblClinVar.1
Natural variantiVAR_076990479D → V in DLDD; reduced dehydrogenase activity; increased proteolytic activity. 2 PublicationsCorresponds to variant dbSNP:rs397514649EnsemblClinVar.1
Natural variantiVAR_076991482R → G in DLDD; reduced enzyme activity. Corresponds to variant dbSNP:rs397514650EnsemblClinVar.1
Natural variantiVAR_006908488P → L in DLDD; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964988EnsemblClinVar.1
Natural variantiVAR_015821495R → G in DLDD; loss of enzyme activity; reduced interaction with PDHX. 3 PublicationsCorresponds to variant dbSNP:rs121964989EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0558551 – 99Missing in isoform 2. 1 PublicationAdd BLAST99
Alternative sequenceiVSP_055856147 – 194Missing in isoform 3. 1 PublicationAdd BLAST48

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

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DDBJi
Links Updated
J03490 mRNA Translation: AAA59527.1
J03620 mRNA Translation: AAA35764.1
L13761
, L13749, L13750, L13751, L13752, L13753, L13754, L13748, L13755, L13759, L13760, L13756, L13757, L13758 Genomic DNA Translation: AAB01381.1
AK295080 mRNA Translation: BAG58122.1
AK300077 mRNA Translation: BAG61881.1
AK312346 mRNA Translation: BAG35267.1
AB209703 mRNA Translation: BAD92940.1 Different initiation.
AC005046 Genomic DNA No translation available.
CH236947 Genomic DNA Translation: EAL24389.1
CH471070 Genomic DNA Translation: EAW83421.1
BC018648 mRNA Translation: AAH18648.1
BC018696 mRNA Translation: AAH18696.1
M99384 Genomic DNA Translation: AAA35759.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS5749.1 [P09622-1]
CCDS78268.1 [P09622-3]

Protein sequence database of the Protein Information Resource

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PIRi
A92622 DEHULP

NCBI Reference Sequences

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RefSeqi
NP_000099.2, NM_000108.4 [P09622-1]
NP_001276679.1, NM_001289750.1 [P09622-2]
NP_001276680.1, NM_001289751.1
NP_001276681.1, NM_001289752.1 [P09622-3]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.131711

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000205402; ENSP00000205402; ENSG00000091140 [P09622-1]
ENST00000417551; ENSP00000390667; ENSG00000091140 [P09622-1]
ENST00000437604; ENSP00000387542; ENSG00000091140 [P09622-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
1738

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1738

UCSC genome browser

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UCSCi
uc003vet.5 human [P09622-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
J03490 mRNA Translation: AAA59527.1
J03620 mRNA Translation: AAA35764.1
L13761
, L13749, L13750, L13751, L13752, L13753, L13754, L13748, L13755, L13759, L13760, L13756, L13757, L13758 Genomic DNA Translation: AAB01381.1
AK295080 mRNA Translation: BAG58122.1
AK300077 mRNA Translation: BAG61881.1
AK312346 mRNA Translation: BAG35267.1
AB209703 mRNA Translation: BAD92940.1 Different initiation.
AC005046 Genomic DNA No translation available.
CH236947 Genomic DNA Translation: EAL24389.1
CH471070 Genomic DNA Translation: EAW83421.1
BC018648 mRNA Translation: AAH18648.1
BC018696 mRNA Translation: AAH18696.1
M99384 Genomic DNA Translation: AAA35759.1
CCDSiCCDS5749.1 [P09622-1]
CCDS78268.1 [P09622-3]
PIRiA92622 DEHULP
RefSeqiNP_000099.2, NM_000108.4 [P09622-1]
NP_001276679.1, NM_001289750.1 [P09622-2]
NP_001276680.1, NM_001289751.1
NP_001276681.1, NM_001289752.1 [P09622-3]
UniGeneiHs.131711

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZMCX-ray2.53A/B/C/D/E/F/G/H36-509[»]
1ZMDX-ray2.08A/B/C/D/E/F/G/H36-509[»]
1ZY8X-ray2.59A/B/C/D/E/F/G/H/I/J36-509[»]
2F5ZX-ray2.18A/B/C/D/E/F/G/H/I/J36-509[»]
3RNMX-ray2.40A/B/C/D36-509[»]
5J5ZX-ray1.84A/B36-509[»]
5NHGX-ray2.27A/B/C/D/E/F/G/H36-509[»]
ProteinModelPortaliP09622
SMRiP09622
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108082, 375 interactors
CORUMiP09622
DIPiDIP-29027N
IntActiP09622, 320 interactors
MINTiP09622
STRINGi9606.ENSP00000205402

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide
DB00157 NADH

PTM databases

iPTMnetiP09622
PhosphoSitePlusiP09622
SwissPalmiP09622

Polymorphism and mutation databases

BioMutaiDLD
DMDMi269849557

2D gel databases

REPRODUCTION-2DPAGEiIPI00015911
UCD-2DPAGEiP09622

Proteomic databases

EPDiP09622
jPOSTiP09622
MaxQBiP09622
PaxDbiP09622
PeptideAtlasiP09622
PRIDEiP09622
ProteomicsDBi52254

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1738
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000205402; ENSP00000205402; ENSG00000091140 [P09622-1]
ENST00000417551; ENSP00000390667; ENSG00000091140 [P09622-1]
ENST00000437604; ENSP00000387542; ENSG00000091140 [P09622-3]
GeneIDi1738
KEGGihsa:1738
UCSCiuc003vet.5 human [P09622-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1738
DisGeNETi1738
EuPathDBiHostDB:ENSG00000091140.12

GeneCards: human genes, protein and diseases

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GeneCardsi
DLD
GeneReviewsiDLD

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0006994
HGNCiHGNC:2898 DLD
HPAiHPA044849
MalaCardsiDLD
MIMi238331 gene
246900 phenotype
neXtProtiNX_P09622
OpenTargetsiENSG00000091140
Orphaneti2394 Pyruvate dehydrogenase E3 deficiency
PharmGKBiPA27352

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1335 Eukaryota
COG1249 LUCA
GeneTreeiENSGT00550000074844
HOGENOMiHOG000276708
HOVERGENiHBG002290
InParanoidiP09622
KOiK00382
OMAiTMSEAVM
OrthoDBi581771at2759
PhylomeDBiP09622
TreeFamiTF300414

Enzyme and pathway databases

BioCyciMetaCyc:HS01727-MONOMER
BRENDAi1.8.1.4 2681
ReactomeiR-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-HSA-389661 Glyoxylate metabolism and glycine degradation
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-6783984 Glycine degradation
R-HSA-70268 Pyruvate metabolism
R-HSA-70895 Branched-chain amino acid catabolism
R-HSA-71064 Lysine catabolism
R-HSA-71403 Citric acid cycle (TCA cycle)
SABIO-RKiP09622

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
DLD human
EvolutionaryTraceiP09622

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Dihydrolipoamide_dehydrogenase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
1738

Protein Ontology

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PROi
PR:P09622

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000091140 Expressed in 234 organ(s), highest expression level in heart right ventricle
CleanExiHS_DLD
ExpressionAtlasiP09622 baseline and differential
GenevisibleiP09622 HS

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 2 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006258 Lipoamide_DH
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
PfamiView protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit
PIRSFiPIRSF000350 Mercury_reductase_MerA, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit
TIGRFAMsiTIGR01350 lipoamide_DH, 1 hit
PROSITEiView protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 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 nameiDLDH_HUMAN
<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: P09622
Secondary accession number(s): B2R5X0
, B4DHG0, B4DT69, Q14131, Q14167, Q59EV8, Q8WTS4
<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 1, 1989
Last sequence update: November 24, 2009
Last modified: January 16, 2019
This is version 229 of the entry and version 2 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 programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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