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Entry version 136 (02 Dec 2020)
Sequence version 1 (05 Jul 2004)
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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

Dld

Organism
Rattus norvegicus (Rat)
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). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. 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. In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).By similarity

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%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

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei89FADBy similarity1
Binding sitei154FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei243NADBy similarity1
Binding sitei278NAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei314NAD; via amide nitrogenBy similarity1
Binding sitei355FADBy 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>Sitei448Important for interaction with PDHX and activity of pyruvate dehydrogenase complexBy similarity1
Sitei473Important for interaction with PDHX and activity of pyruvate dehydrogenase complexBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei487Proton acceptorBy 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 bindingi71 – 80FADBy similarity10
Nucleotide bindingi183 – 185FADBy similarity3
Nucleotide bindingi220 – 227NADBy similarity8
Nucleotide bindingi361 – 364FADBy similarity4

<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

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q6P6R2

<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:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4By similarity)
Alternative name(s):
Dihydrolipoamide dehydrogenase
<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:Dld
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 6

Organism-specific databases

Rat genome database

More...
RGDi
735073, Dld

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

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

<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 – 35MitochondrionBy similarityAdd BLAST35
<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_000026022836 – 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; alternateBy similarity1
Modified residuei143N6-succinyllysine; alternateBy similarity1
Modified residuei159N6-succinyllysineBy similarity1
Modified residuei273N6-succinyllysineBy similarity1
Modified residuei277N6-succinyllysineBy similarity1
Modified residuei285PhosphoserineBy similarity1
Modified residuei297PhosphoserineCombined sources1
Modified residuei346N6-acetyllysineBy similarity1
Modified residuei410N6-acetyllysine; alternateBy similarity1
Modified residuei410N6-succinyllysine; alternateBy similarity1
Modified residuei417N6-acetyllysineBy similarity1
Modified residuei420N6-acetyllysineBy similarity1
Modified residuei430N6-succinyllysineBy similarity1
Modified residuei502PhosphoserineBy similarity1
Modified residuei505N6-acetyllysine; alternateBy similarity1
Modified residuei505N6-succinyllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q6P6R2

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

More...
PaxDbi
Q6P6R2

PRoteomics IDEntifications database

More...
PRIDEi
Q6P6R2

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6P6R2

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

More...
PhosphoSitePlusi
Q6P6R2

<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

More...
Bgeei
ENSRNOG00000006364, Expressed in heart and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q6P6R2, RN

<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

Homodimer. 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). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (by non covalent bonds). 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.

Interacts with PDHX.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
256067, 2 interactors

Protein interaction database and analysis system

More...
IntActi
Q6P6R2, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000008980

<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
Q6P6R2

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

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1335, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074844

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_016755_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6P6R2

Identification of Orthologs from Complete Genome Data

More...
OMAi
TMSEAVM

Database of Orthologous Groups

More...
OrthoDBi
581771at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6P6R2

TreeFam database of animal gene trees

More...
TreeFami
TF300414

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.390.30, 1 hit
3.50.50.60, 2 hits

Integrated resource of protein families, domains and functional sites

More...
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

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000350, Mercury_reductase_MerA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51905, SSF51905, 1 hit
SSF55424, SSF55424, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01350, lipoamide_DH, 1 hit

PROSITE; a protein domain and family database

More...
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%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.

<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 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.

Q6P6R2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQSWSRVYCS LAKKGHFNRL SHGLQGASSV PLRTYSDQPI DADVTVIGSG
60 70 80 90 100
PGGYVAAIKA AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHL
110 120 130 140 150
AHGKDFASRG IEIPEVRLNL EKMMEQKRSA VKALTGGIAH LFKQNKVVHV
160 170 180 190 200
NGFGKITGKN QVTATTADGS TQVIGTKNIL IATGSEVTPF PGITIDEDTI
210 220 230 240 250
VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG
260 270 280 290 300
IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK
310 320 330 340 350
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN TRFQTKIPNI
360 370 380 390 400
FAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA
410 420 430 440 450
WVGKSEEQLK EEGVEFKVGK FPFAANSRAK TNADTDGMVK ILGHKSTDRI
460 470 480 490 500
LGAHILGPGA GEMVNEAALA LEYGASCEDV ARVCHAHPTL SEAFREANLA

ASFGKPINF
Length:509
Mass (Da):54,038
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:i854802DBFE36573A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BC062069 mRNA Translation: AAH62069.1

NCBI Reference Sequences

More...
RefSeqi
NP_955417.1, NM_199385.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000008980; ENSRNOP00000008980; ENSRNOG00000006364

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
298942

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:298942

UCSC genome browser

More...
UCSCi
RGD:735073, rat

<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
BC062069 mRNA Translation: AAH62069.1
RefSeqiNP_955417.1, NM_199385.2

3D structure databases

SMRiQ6P6R2
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi256067, 2 interactors
IntActiQ6P6R2, 1 interactor
STRINGi10116.ENSRNOP00000008980

PTM databases

iPTMnetiQ6P6R2
PhosphoSitePlusiQ6P6R2

Proteomic databases

jPOSTiQ6P6R2
PaxDbiQ6P6R2
PRIDEiQ6P6R2

Genome annotation databases

EnsembliENSRNOT00000008980; ENSRNOP00000008980; ENSRNOG00000006364
GeneIDi298942
KEGGirno:298942
UCSCiRGD:735073, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1738
RGDi735073, Dld

Phylogenomic databases

eggNOGiKOG1335, Eukaryota
GeneTreeiENSGT00550000074844
HOGENOMiCLU_016755_0_1_1
InParanoidiQ6P6R2
OMAiTMSEAVM
OrthoDBi581771at2759
PhylomeDBiQ6P6R2
TreeFamiTF300414

Enzyme and pathway databases

ReactomeiR-RNO-204174, Regulation of pyruvate dehydrogenase (PDH) complex
R-RNO-389661, Glyoxylate metabolism and glycine degradation
R-RNO-5362517, Signaling by Retinoic Acid
R-RNO-6783984, Glycine degradation
R-RNO-70268, Pyruvate metabolism
R-RNO-70895, Branched-chain amino acid catabolism
R-RNO-71064, Lysine catabolism
R-RNO-71403, Citric acid cycle (TCA cycle)
SABIO-RKiQ6P6R2

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q6P6R2

Gene expression databases

BgeeiENSRNOG00000006364, Expressed in heart and 21 other tissues
GenevisibleiQ6P6R2, RN

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...

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 nameiDLDH_RAT
<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: Q6P6R2
<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: November 28, 2006
Last sequence update: July 5, 2004
Last modified: December 2, 2020
This is version 136 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 programChordata 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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