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Q9HUY1 (DLDH3_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase 3
EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase 3
Short name=LPD-3
Gene names
Name:lpd3
Ordered Locus Names:PA4829
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

LPD-3 may substitute for lipoamide dehydrogenase of the 2-oxoglutarate dehydrogenase and pyruvate multienzyme complexes when the latter is inactive or missing By similarity.

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond By similarity.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Dihydrolipoyl dehydrogenase 3
PRO_0000287806

Regions

Nucleotide binding34 – 4310FAD By similarity
Nucleotide binding182 – 1865NAD By similarity
Nucleotide binding272 – 2754NAD By similarity

Sites

Active site4461Proton acceptor By similarity
Binding site521FAD By similarity
Binding site1161FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2051NAD By similarity
Binding site2391NAD; via amide nitrogen By similarity
Binding site3141FAD By similarity
Binding site3221FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond43 ↔ 48Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HUY1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 0DC0AACBF6D86A8C

FASTA46749,659
        10         20         30         40         50         60 
MMESYDVIVI GAGPGGYNAA IRAGQLGLKV ACVEGRETLG GTCLNVGCMP SKALLHASEL 

        70         80         90        100        110        120 
YAAASGGEFA RLGIRVSPEL DLAQMMKQKD ESVAALTRGV EFLFRKHKVQ WIKGWARLQG 

       130        140        150        160        170        180 
EGRVGVALAD GGHAQLEARD IVIATGSEPA PLPGVPVDNQ RILDSTGALE LVEVPRHLVV 

       190        200        210        220        230        240 
IGAGVIGLEL GSVWRRLGAQ VTVLEYLERI CPGLDGETAR TLQRALTRQG MRFRLGTRVV 

       250        260        270        280        290        300 
AARSGEQGVE LDLQPAAGGA TESLQADYVL VAIGRRPYTE GLGLETVGLA SDRRGMLENQ 

       310        320        330        340        350        360 
GQRSAAPGVW VIGDVTSGPM LAHKAEEEAI VCIERIAGHA AEMNAEVIPS VIYTQPEVAS 

       370        380        390        400        410        420 
VGLGEEQLQA ARREYKVGRF PFSANSRAKI NHESEGFIKI LSDARSDQVL GVHMIGPGVS 

       430        440        450        460 
EMIGEACVAM EFSASAEDLA LTCHPHPTRS EALRQAAMDV HGRAMQN

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004091 Genomic DNA. Translation: AAG08214.1.
PIRA83042.
RefSeqNP_253516.1. NC_002516.2.

3D structure databases

HSSPHSSP built from PDB template 2F5Z based on UniProtKB P09622.
ProteinModelPortalQ9HUY1.
SMRQ9HUY1. Positions 5-458.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA4829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID882254.
KEGGpae:PA4829.
PATRIC19844457. VBIPseAer58763_5060.

Organism-specific databases

PseudoCAPPA4829.

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276708.
KOK00382.
OMAHIVGFGA.
ProtClustDBPRK06115.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PANTHERPTHR22912:SF20. PTHR22912:SF20. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH3_PSEAE
AccessionPrimary (citable) accession number: Q9HUY1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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