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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781FADBy similarity
Binding sitei142 – 1421FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei230 – 2301NADBy similarity
Binding sitei264 – 2641NAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei302 – 3021NAD; via amide nitrogenBy similarity
Binding sitei343 – 3431FADBy similarity
Active sitei475 – 4751Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi60 – 6910FADBy similarity
Nucleotide bindingi170 – 1723FADBy similarity
Nucleotide bindingi207 – 2148NADBy similarity
Nucleotide bindingi349 – 3524FADBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 497497Dihydrolipoyl dehydrogenasePRO_0000068007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi69 ↔ 74Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO18480.
SMRiO18480. Positions 30-497.
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.
SMRiO18480. Positions 30-497.
ModBaseiSearch...
MobiDBiSearch...

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...

Publicationsi

  1. "Primary structure of an invertebrate dihydrolipoamide dehydrogenase with phylogenetic relationship to vertebrate and bacterial disulfide oxidoreductases."
    Pullikuth A.K., Gill S.S.
    Gene 200:163-172(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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: November 11, 2015
This is version 97 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.