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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581FAD1 Publication
Binding sitei122 – 1221FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei211 – 2111NADBy similarity
Binding sitei245 – 2451NAD; via amide nitrogenBy similarity
Binding sitei319 – 3191FAD1 Publication
Binding sitei327 – 3271FAD; via amide nitrogen1 Publication
Active sitei451 – 4511Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 4916FAD1 PublicationAdd
BLAST
Nucleotide bindingi188 – 1925NADBy similarity
Nucleotide bindingi276 – 2794NADBy 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

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

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Dihydrolipoyl dehydrogenasePRO_0000068014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi14 – 2613Combined sources
Beta strandi30 – 345Combined sources
Beta strandi41 – 433Combined sources
Helixi47 – 526Combined sources
Helixi54 – 7118Combined sources
Helixi75 – 773Combined sources
Helixi88 – 11326Combined sources
Beta strandi116 – 1249Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi165 – 1706Combined sources
Helixi171 – 1744Combined sources
Beta strandi182 – 1876Combined sources
Helixi191 – 20212Combined sources
Beta strandi206 – 21712Combined sources
Helixi222 – 23413Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi244 – 2507Combined sources
Beta strandi255 – 27521Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi314 – 3163Combined sources
Helixi318 – 3203Combined sources
Beta strandi321 – 3233Combined sources
Helixi327 – 34317Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi359 – 3679Combined sources
Helixi370 – 3756Combined sources
Beta strandi380 – 3867Combined sources
Helixi387 – 3893Combined sources
Helixi391 – 3966Combined sources
Beta strandi402 – 4087Combined sources
Turni409 – 4113Combined sources
Beta strandi413 – 4219Combined sources
Helixi424 – 43613Combined sources
Helixi441 – 4455Combined sources
Helixi455 – 46511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LADX-ray2.20A/B2-477[»]
ProteinModelPortaliP18925.
SMRiP18925. Positions 2-473.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
3LADX-ray2.20A/B2-477[»]
ProteinModelPortaliP18925.
SMRiP18925. Positions 2-473.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_29750.

Chemistry

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 11, 2015
This is version 118 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.