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Protein

Dihydrolipoyl dehydrogenase

Gene

pdhD

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes.

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 sitei56FAD1 Publication1
Binding sitei119FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei206NADBy similarity1
Binding sitei314FAD1 Publication1
Binding sitei322FAD; via amide nitrogen1 Publication1
Active sitei446Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi39 – 47FAD1 Publication9
Nucleotide bindingi183 – 187NADBy similarity5
Nucleotide bindingi271 – 274NADBy 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

BRENDAi1.8.1.4. 623.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of pyruvate complex
Gene namesi
Name:pdhD
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680151 – 470Dihydrolipoyl dehydrogenaseAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47 ↔ 52Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer. Identified in a complex with PdhC.1 Publication

Protein-protein interaction databases

DIPiDIP-6155N.

Structurei

Secondary structure

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 15Combined sources5
Helixi19 – 30Combined sources12
Beta strandi35 – 41Combined sources7
Helixi45 – 49Combined sources5
Helixi52 – 69Combined sources18
Helixi72 – 74Combined sources3
Helixi85 – 108Combined sources24
Turni109 – 111Combined sources3
Beta strandi113 – 123Combined sources11
Beta strandi126 – 131Combined sources6
Beta strandi134 – 139Combined sources6
Beta strandi141 – 145Combined sources5
Beta strandi149 – 151Combined sources3
Beta strandi161 – 164Combined sources4
Helixi166 – 170Combined sources5
Beta strandi177 – 182Combined sources6
Helixi186 – 197Combined sources12
Beta strandi201 – 212Combined sources12
Helixi217 – 229Combined sources13
Beta strandi233 – 246Combined sources14
Beta strandi249 – 256Combined sources8
Beta strandi259 – 270Combined sources12
Beta strandi274 – 277Combined sources4
Beta strandi279 – 282Combined sources4
Turni283 – 287Combined sources5
Beta strandi309 – 311Combined sources3
Helixi313 – 315Combined sources3
Beta strandi316 – 318Combined sources3
Helixi322 – 336Combined sources15
Beta strandi350 – 352Combined sources3
Beta strandi354 – 356Combined sources3
Beta strandi358 – 362Combined sources5
Helixi365 – 369Combined sources5
Turni370 – 372Combined sources3
Beta strandi375 – 381Combined sources7
Helixi382 – 384Combined sources3
Helixi386 – 391Combined sources6
Beta strandi397 – 403Combined sources7
Turni404 – 406Combined sources3
Beta strandi408 – 416Combined sources9
Helixi419 – 432Combined sources14
Helixi436 – 441Combined sources6
Helixi451 – 459Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBDX-ray2.60A/B7-461[»]
ProteinModelPortaliP11959.
SMRiP11959.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11959.

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.

P11959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVGDFAIET ETLVVGAGPG GYVAAIRAAQ LGQKVTIVEK GNLGGVCLNV
60 70 80 90 100
GCIPSKALIS ASHRYEQAKH SEEMGIKAEN VTIDFAKVQE WKASVVKKLT
110 120 130 140 150
GGVEGLLKGN KVEIVKGEAY FVDANTVRVV NGDSAQTYTF KNAIIATGSR
160 170 180 190 200
PIELPNFKFS NRILDSTGAL NLGEVPKSLV VIGGGYIGIE LGTAYANFGT
210 220 230 240 250
KVTILEGAGE ILSGFEKQMA AIIKKRLKKK GVEVVTNALA KGAEEREDGV
260 270 280 290 300
TVTYEANGET KTIDADYVLV TVGRRPNTDE LGLEQIGIKM TNRGLIEVDQ
310 320 330 340 350
QCRTSVPNIF AIGDIVPGPA LAHKASYEGK VAAEAIAGHP SAVDYVAIPA
360 370 380 390 400
VVFSDPECAS VGYFEQQAKD EGIDVIAAKF PFAANGRALA LNDTDGFLKL
410 420 430 440 450
VVRKEDGVII GAQIIGPNAS DMIAELGLAI EAGMTAEDIA LTIHAHPTLG
460 470
EIAMEAAEVA LGTPIHIITK
Length:470
Mass (Da):49,356
Last modified:May 1, 1991 - v2
Checksum:iC9C05F21A3EE4CB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37631.1.
PIRiS13839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37631.1.
PIRiS13839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBDX-ray2.60A/B7-461[»]
ProteinModelPortaliP11959.
SMRiP11959.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6155N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.8.1.4. 623.

Miscellaneous databases

EvolutionaryTraceiP11959.

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 nameiDLDH1_GEOSE
AccessioniPrimary (citable) accession number: P11959
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 1, 1991
Last modified: November 2, 2016
This is version 126 of the entry and version 2 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.