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Protein

Dihydrolipoyl dehydrogenase

Gene
N/A
Organism
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei78FADBy similarity1
Binding sitei142FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei230NADBy similarity1
Binding sitei264NAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei302NAD; via amide nitrogenBy similarity1
Binding sitei343FADBy similarity1
Active sitei475Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi60 – 69FADBy similarity10
Nucleotide bindingi170 – 172FADBy similarity3
Nucleotide bindingi207 – 214NADBy similarity8
Nucleotide bindingi349 – 352FADBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3
OrganismiManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifieri7130 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680071 – 497Dihydrolipoyl dehydrogenaseAdd BLAST497

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi69 ↔ 74Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiO18480.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO18480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O18480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGYKFLKLAS ASFRNGGVRI VSRQYSTTHD ADLVVIGAGP GGYVAAIKAA
60 70 80 90 100
QLGMKVVSVE KEPSLGGTCL NVGCIPSKAL LHNTHLYHMA KHDFKHRGIE
110 120 130 140 150
TGEVKFNFKA MMDYKVNAVK ALTGGIAMLF QKNKVKLVRG AGTIVAPNKV
160 170 180 190 200
EVKGEKGVET VNTKNILIAT GSEVTPFPGV TFDEKQIITS TGALSLESVP
210 220 230 240 250
KKMLVIGAGV IGLELGSVYQ RLGADVTAIE FLGSIGGIGI DMEVSKDYRI
260 270 280 290 300
LAKQGMKFKL ETKVLGVKKE GSTVKVEDVS IEGAKGGNKE TMDCDVVLIS
310 320 330 340 350
IGRRPYTKDL GLDKVGIALD DRGRVPVNNK FQTTVPGIYA IGDVIHGPML
360 370 380 390 400
AHKAEDEGIV CVEGIKGMPV HFNYDAIPSV IYTSPEVGWV RKTEEDLKKE
410 420 430 440 450
GKAYKVRKFP FLANSRAKTN GEPDGFVKVL SDKATDVILG THIIGPGGGE
460 470 480 490
LINEAVLAQE YGAAAEDVAR VCHAHPTCAE ALREANLAAY CGKPINF
Length:497
Mass (Da):53,083
Last modified:January 1, 1998 - v1
Checksum:i1689E564E165137A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008586 mRNA. Translation: AAB88282.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008586 mRNA. Translation: AAB88282.1.

3D structure databases

ProteinModelPortaliO18480.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO18480.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDLDH_MANSE
AccessioniPrimary (citable) accession number: O18480
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: October 5, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.