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Protein

Dihydrolipoyl dehydrogenase

Gene

lpd

Organism
Pseudomonas fluorescens
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (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 oxygen1 Publication1
Binding sitei211NADBy similarity1
Binding sitei245NAD; via amide nitrogenBy similarity1
Binding sitei319FAD1 Publication1
Binding sitei327FAD; via amide nitrogen1 Publication1
Active sitei451Proton acceptorBy similarity1

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

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of 2-oxoglutarate dehydrogenase complex
Gene namesi
Name:lpd
OrganismiPseudomonas fluorescens
Taxonomic identifieri294 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

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
Initiator methionineiRemoved1 Publication
ChainiPRO_00000680372 – 478Dihydrolipoyl dehydrogenaseAdd BLAST477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 54Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP14218.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi14 – 25Combined sources12
Beta strandi30 – 34Combined sources5
Beta strandi39 – 43Combined sources5
Helixi47 – 52Combined sources6
Helixi54 – 72Combined sources19
Helixi75 – 77Combined sources3
Beta strandi79 – 86Combined sources8
Helixi88 – 113Combined sources26
Beta strandi115 – 124Combined sources10
Helixi126 – 128Combined sources3
Beta strandi129 – 134Combined sources6
Beta strandi139 – 149Combined sources11
Beta strandi153 – 155Combined sources3
Turni165 – 167Combined sources3
Helixi171 – 174Combined sources4
Beta strandi182 – 187Combined sources6
Helixi191 – 202Combined sources12
Beta strandi206 – 210Combined sources5
Beta strandi212 – 217Combined sources6
Helixi222 – 235Combined sources14
Beta strandi238 – 240Combined sources3
Beta strandi244 – 247Combined sources4
Beta strandi254 – 260Combined sources7
Beta strandi265 – 271Combined sources7
Beta strandi273 – 275Combined sources3
Beta strandi279 – 281Combined sources3
Turni284 – 286Combined sources3
Beta strandi308 – 311Combined sources4
Beta strandi314 – 316Combined sources3
Helixi318 – 320Combined sources3
Beta strandi321 – 323Combined sources3
Helixi327 – 341Combined sources15
Helixi350 – 352Combined sources3
Beta strandi355 – 357Combined sources3
Beta strandi359 – 367Combined sources9
Helixi370 – 375Combined sources6
Beta strandi380 – 386Combined sources7
Helixi387 – 389Combined sources3
Helixi391 – 396Combined sources6
Beta strandi402 – 411Combined sources10
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
1LPFX-ray2.80A/B2-478[»]
ProteinModelPortaliP14218.
SMRiP14218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14218.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKFDVVVI GAGPGGYVAA IRAAQLGLKT ACIEKYIGKE GKVALGGTCL
60 70 80 90 100
NVGCIPSKAL LDSSYKYHEA KEAFKVHGIE AKGVTIDVPA MVARKANIVK
110 120 130 140 150
NLTGGIATLF KANGVTSFEG HGKLLANKQV EVTGLDGKTQ VLEAENVIIA
160 170 180 190 200
SGSRPVEIPP APLSDDIIVD STGALEFQAV PKKLGVIGAG VIGLELGSVW
210 220 230 240 250
ARLGAEVTVL EALDKFLPAA DEQIAKEALK VLTKQGLNIR LGARVTASEV
260 270 280 290 300
KKKQVTVTFT DANGEQKETF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF
310 320 330 340 350
IYVDDHCKTS VPGVFAIGDV VRGAMLAHKA SEEGVMVAER IAGHKAQMNY
360 370 380 390 400
DLIPSVIYTH PEIAWVGKTE QTLKAEGVEV NVGTFPFAAS GRAMAANDTT
410 420 430 440 450
GLVKVIADAK TDRVLGVHVI GPSAAELVQQ GAIGMEFGTS AEDLGMMVFS
460 470
HPTLSEALHE AALAVNGHAI HIANRKKR
Length:478
Mass (Da):50,151
Last modified:January 23, 2007 - v3
Checksum:iB23EB31268C69EC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28356 Genomic DNA. Translation: AAA99234.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28356 Genomic DNA. Translation: AAA99234.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LPFX-ray2.80A/B2-478[»]
ProteinModelPortaliP14218.
SMRiP14218.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PRIDEiP14218.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP14218.

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_PSEFL
AccessioniPrimary (citable) accession number: P14218
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 126 of the entry and version 3 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, Direct protein sequencing

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.