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Protein

Dihydrolipoyl dehydrogenase

Gene
N/A
Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activityi

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

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei58FAD1 Publication1
Binding sitei122FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei211NADBy similarity1
Binding sitei245NAD; via amide nitrogenBy similarity1
Binding sitei319FAD1 Publication1
Binding sitei327FAD; via amide nitrogen1 Publication1
Active sitei451Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi34 – 49FAD1 PublicationAdd BLAST16
Nucleotide bindingi188 – 192NADBy similarity5
Nucleotide bindingi276 – 279NADBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

SABIO-RKP18925.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of pyruvate complex
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680141 – 477Dihydrolipoyl dehydrogenaseAdd BLAST477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 54Redox-active2 Publications

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi322710.Avin_29750.

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Helixi14 – 26Combined sources13
Beta strandi30 – 34Combined sources5
Beta strandi41 – 43Combined sources3
Helixi47 – 52Combined sources6
Helixi54 – 71Combined sources18
Helixi75 – 77Combined sources3
Helixi88 – 113Combined sources26
Beta strandi116 – 124Combined sources9
Beta strandi130 – 133Combined sources4
Beta strandi139 – 142Combined sources4
Beta strandi147 – 149Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi165 – 170Combined sources6
Helixi171 – 174Combined sources4
Beta strandi182 – 187Combined sources6
Helixi191 – 202Combined sources12
Beta strandi206 – 217Combined sources12
Helixi222 – 234Combined sources13
Beta strandi237 – 241Combined sources5
Beta strandi244 – 250Combined sources7
Beta strandi255 – 275Combined sources21
Beta strandi279 – 281Combined sources3
Beta strandi314 – 316Combined sources3
Helixi318 – 320Combined sources3
Beta strandi321 – 323Combined sources3
Helixi327 – 343Combined sources17
Beta strandi355 – 357Combined sources3
Beta strandi359 – 367Combined sources9
Helixi370 – 375Combined sources6
Beta strandi380 – 386Combined sources7
Helixi387 – 389Combined sources3
Helixi391 – 396Combined sources6
Beta strandi402 – 408Combined sources7
Turni409 – 411Combined sources3
Beta strandi413 – 421Combined sources9
Helixi424 – 436Combined sources13
Helixi441 – 445Combined sources5
Helixi455 – 465Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LADX-ray2.20A/B2-477[»]
ProteinModelPortaliP18925.
SMRiP18925.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18925.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.

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.

P18925-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKFDVIVI GAGPGGYVAA IKSAQLGLKT ALIEKYKGKE GKTALGGTCL
60 70 80 90 100
NVGCIPSKAL LDSSYKFHEA HESFKLHGIS TGEVAIDVPT MIARKDQIVR
110 120 130 140 150
NLTGGVASLI KANGVTLFEG HGKLLAGKKV EVTAADGSSQ VLDTENVILA
160 170 180 190 200
SGSKPVEIPP APVDQDVIVD STGALDFQNV PGKLGVIGAG VIGLELGSVW
210 220 230 240 250
ARLGAEVTVL EAMDKFLPAV DEQVAKEAQK ILTKQGLKIL LGARVTGTEV
260 270 280 290 300
KNKQVTVKFV DAEGEKSQAF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF
310 320 330 340 350
IYVDDYCATS VPGVYAIGDV VRGAMLAHKA SEEGVVVAER IAGHKAQMNY
360 370 380 390 400
DLIPAVIYTH PEIAGVGKTE QALKAEGVAI NVGVFPFAAS GRAMAANDTA
410 420 430 440 450
GFVKVIADAK TDRVLGVHVI GPSAAELVQQ GAIAMEFGTS AEDLGMMVFA
460 470
HPALSEALHE AALAVSGHAI HVANRKK
Length:477
Mass (Da):49,567
Last modified:November 1, 1990 - v1
Checksum:i4219A8EA4DAFCAD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37307 Genomic DNA. Translation: AAA22139.1.
X52432 Genomic DNA. Translation: CAA36679.1.
PIRiS00360. DEAVHL.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37307 Genomic DNA. Translation: AAA22139.1.
X52432 Genomic DNA. Translation: CAA36679.1.
PIRiS00360. DEAVHL.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LADX-ray2.20A/B2-477[»]
ProteinModelPortaliP18925.
SMRiP18925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_29750.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.

Enzyme and pathway databases

SABIO-RKP18925.

Miscellaneous databases

EvolutionaryTraceiP18925.

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_AZOVI
AccessioniPrimary (citable) accession number: P18925
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.