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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561FAD1 Publication
Binding sitei119 – 1191FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei206 – 2061NADBy similarity
Binding sitei314 – 3141FAD1 Publication
Binding sitei322 – 3221FAD; via amide nitrogen1 Publication
Active sitei446 – 4461Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 479FAD1 Publication
Nucleotide bindingi183 – 1875NADBy similarity
Nucleotide bindingi271 – 2744NADBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Dihydrolipoyl dehydrogenasePRO_0000068015Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 155Combined sources
Helixi19 – 3012Combined sources
Beta strandi35 – 417Combined sources
Helixi45 – 495Combined sources
Helixi52 – 6918Combined sources
Helixi72 – 743Combined sources
Helixi85 – 10824Combined sources
Turni109 – 1113Combined sources
Beta strandi113 – 12311Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi161 – 1644Combined sources
Helixi166 – 1705Combined sources
Beta strandi177 – 1826Combined sources
Helixi186 – 19712Combined sources
Beta strandi201 – 21212Combined sources
Helixi217 – 22913Combined sources
Beta strandi233 – 24614Combined sources
Beta strandi249 – 2568Combined sources
Beta strandi259 – 27012Combined sources
Beta strandi274 – 2774Combined sources
Beta strandi279 – 2824Combined sources
Turni283 – 2875Combined sources
Beta strandi309 – 3113Combined sources
Helixi313 – 3153Combined sources
Beta strandi316 – 3183Combined sources
Helixi322 – 33615Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi358 – 3625Combined sources
Helixi365 – 3695Combined sources
Turni370 – 3723Combined sources
Beta strandi375 – 3817Combined sources
Helixi382 – 3843Combined sources
Helixi386 – 3916Combined sources
Beta strandi397 – 4037Combined sources
Turni404 – 4063Combined sources
Beta strandi408 – 4169Combined sources
Helixi419 – 43214Combined sources
Helixi436 – 4416Combined sources
Helixi451 – 4599Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EBDX-ray2.60A/B7-461[»]
ProteinModelPortaliP11959.
SMRiP11959. Positions 7-461.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1EBDX-ray2.60A/B7-461[»]
ProteinModelPortaliP11959.
SMRiP11959. Positions 7-461.
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 11, 2015
This is version 124 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.