UniProtKB - Q6P6R2 (DLDH_RAT)
Dihydrolipoyl dehydrogenase, mitochondrial
Dld
Functioni
Miscellaneous
Catalytic activityi
- (R)-N6-dihydrolipoyl-L-lysyl-[protein] + NAD+ = (R)-N6-lipoyl-L-lysyl-[protein] + H+ + NADHBy similarityEC:1.8.1.4By similarity
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 89 | FADBy similarity | 1 | |
Binding sitei | 154 | FAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 243 | NADBy similarity | 1 | |
Binding sitei | 278 | NAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 314 | NAD; via amide nitrogenBy similarity | 1 | |
Binding sitei | 355 | FADBy similarity | 1 | |
Sitei | 448 | Important for interaction with PDHX and activity of pyruvate dehydrogenase complexBy similarity | 1 | |
Sitei | 473 | Important for interaction with PDHX and activity of pyruvate dehydrogenase complexBy similarity | 1 | |
Active sitei | 487 | Proton acceptorBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 71 – 80 | FADBy similarity | 10 | |
Nucleotide bindingi | 183 – 185 | FADBy similarity | 3 | |
Nucleotide bindingi | 220 – 227 | NADBy similarity | 8 | |
Nucleotide bindingi | 361 – 364 | FADBy similarity | 4 |
GO - Molecular functioni
- dihydrolipoyl dehydrogenase activity Source: RGD
- flavin adenine dinucleotide binding Source: RGD
- lipoamide binding Source: RGD
- NAD binding Source: RGD
- pyruvate dehydrogenase (NAD+) activity Source: Ensembl
GO - Biological processi
- 2-oxoglutarate metabolic process Source: RGD
- acetyl-CoA biosynthetic process from pyruvate Source: RGD
- aging Source: RGD
- cell redox homeostasis Source: InterPro
- dihydrolipoamide metabolic process Source: RGD
- gastrulation Source: RGD
- histone succinylation Source: UniProtKB
- lipoate metabolic process Source: RGD
- mitochondrial electron transport, NADH to ubiquinone Source: RGD
- oxidation-reduction process Source: GO_Central
- proteolysis Source: RGD
- regulation of membrane potential Source: RGD
- sperm capacitation Source: RGD
Keywordsi
Molecular function | Oxidoreductase |
Ligand | FAD, Flavoprotein, NAD |
Enzyme and pathway databases
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-RKi | Q6P6R2 |
Names & Taxonomyi
Protein namesi | Recommended name: Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4By similarity)Alternative name(s): Dihydrolipoamide dehydrogenase |
Gene namesi | Name:Dld |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 735073, Dld |
Subcellular locationi
Mitochondrion
- Mitochondrion matrix By similarity
Nucleus
- Nucleus By similarity
Other locations
Note: Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation.By similarity
Mitochondrion
- mitochondrial matrix Source: UniProtKB-SubCell
- mitochondrion Source: RGD
Nucleus
- nucleoplasm Source: Ensembl
- nucleus Source: UniProtKB
Other locations
- acrosomal matrix Source: RGD
- cilium Source: RGD
- motile cilium Source: UniProtKB-SubCell
- oxoglutarate dehydrogenase complex Source: RGD
- pyruvate dehydrogenase complex Source: RGD
Keywords - Cellular componenti
Cell projection, Cilium, Cytoplasmic vesicle, Flagellum, Mitochondrion, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 35 | MitochondrionBy similarityAdd BLAST | 35 | |
ChainiPRO_0000260228 | 36 – 509 | Dihydrolipoyl dehydrogenase, mitochondrialAdd BLAST | 474 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 66 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 66 | N6-succinyllysine; alternateBy similarity | 1 | |
Disulfide bondi | 80 ↔ 85 | Redox-activeBy similarity | ||
Modified residuei | 104 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 104 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 122 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 122 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 132 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 132 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 143 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 143 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 159 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 273 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 277 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 285 | PhosphoserineBy similarity | 1 | |
Modified residuei | 297 | PhosphoserineCombined sources | 1 | |
Modified residuei | 346 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 410 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 410 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 417 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 420 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 430 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 502 | PhosphoserineBy similarity | 1 | |
Modified residuei | 505 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 505 | N6-succinyllysine; alternateBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Disulfide bond, PhosphoproteinProteomic databases
jPOSTi | Q6P6R2 |
PaxDbi | Q6P6R2 |
PRIDEi | Q6P6R2 |
PTM databases
iPTMneti | Q6P6R2 |
PhosphoSitePlusi | Q6P6R2 |
Expressioni
Gene expression databases
Bgeei | ENSRNOG00000006364, Expressed in heart and 21 other tissues |
Genevisiblei | Q6P6R2, RN |
Interactioni
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 similarityProtein-protein interaction databases
BioGRIDi | 256067, 2 interactors |
IntActi | Q6P6R2, 1 interactor |
STRINGi | 10116.ENSRNOP00000008980 |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Redox-active center, Transit peptidePhylogenomic databases
eggNOGi | KOG1335, Eukaryota |
GeneTreei | ENSGT00550000074844 |
HOGENOMi | CLU_016755_0_1_1 |
InParanoidi | Q6P6R2 |
OMAi | TMSEAVM |
OrthoDBi | 581771at2759 |
PhylomeDBi | Q6P6R2 |
TreeFami | TF300414 |
Family and domain databases
Gene3Di | 3.30.390.30, 1 hit 3.50.50.60, 2 hits |
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 |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit PF02852, Pyr_redox_dim, 1 hit |
PIRSFi | PIRSF000350, Mercury_reductase_MerA, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF55424, SSF55424, 1 hit |
TIGRFAMsi | TIGR01350, lipoamide_DH, 1 hit |
PROSITEi | View protein in PROSITE PS00076, PYRIDINE_REDOX_1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC062069 mRNA Translation: AAH62069.1 |
RefSeqi | NP_955417.1, NM_199385.2 |
Genome annotation databases
Ensembli | ENSRNOT00000008980; ENSRNOP00000008980; ENSRNOG00000006364 |
GeneIDi | 298942 |
KEGGi | rno:298942 |
UCSCi | RGD:735073, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC062069 mRNA Translation: AAH62069.1 |
RefSeqi | NP_955417.1, NM_199385.2 |
3D structure databases
SMRi | Q6P6R2 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 256067, 2 interactors |
IntActi | Q6P6R2, 1 interactor |
STRINGi | 10116.ENSRNOP00000008980 |
PTM databases
iPTMneti | Q6P6R2 |
PhosphoSitePlusi | Q6P6R2 |
Proteomic databases
jPOSTi | Q6P6R2 |
PaxDbi | Q6P6R2 |
PRIDEi | Q6P6R2 |
Genome annotation databases
Ensembli | ENSRNOT00000008980; ENSRNOP00000008980; ENSRNOG00000006364 |
GeneIDi | 298942 |
KEGGi | rno:298942 |
UCSCi | RGD:735073, rat |
Organism-specific databases
CTDi | 1738 |
RGDi | 735073, Dld |
Phylogenomic databases
eggNOGi | KOG1335, Eukaryota |
GeneTreei | ENSGT00550000074844 |
HOGENOMi | CLU_016755_0_1_1 |
InParanoidi | Q6P6R2 |
OMAi | TMSEAVM |
OrthoDBi | 581771at2759 |
PhylomeDBi | Q6P6R2 |
TreeFami | TF300414 |
Enzyme and pathway databases
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-RKi | Q6P6R2 |
Miscellaneous databases
PROi | PR:Q6P6R2 |
Gene expression databases
Bgeei | ENSRNOG00000006364, Expressed in heart and 21 other tissues |
Genevisiblei | Q6P6R2, RN |
Family and domain databases
Gene3Di | 3.30.390.30, 1 hit 3.50.50.60, 2 hits |
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 |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit PF02852, Pyr_redox_dim, 1 hit |
PIRSFi | PIRSF000350, Mercury_reductase_MerA, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF55424, SSF55424, 1 hit |
TIGRFAMsi | TIGR01350, lipoamide_DH, 1 hit |
PROSITEi | View protein in PROSITE PS00076, PYRIDINE_REDOX_1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DLDH_RAT | |
Accessioni | Q6P6R2Primary (citable) accession number: Q6P6R2 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families