Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9I1L9 (DLDH1_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase
EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of branched-chain alpha-keto acid dehydrogenase complex
LPD-Val
Gene names
Name:lpdV
Ordered Locus Names:PA2250
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 length464 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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) By similarity.

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. UniProtKB P18925

Cofactor

Binds 1 FAD per subunit By similarity. UniProtKB P18925

Subunit structure

Homodimer By similarity. UniProtKB P18925

Subcellular location

Cytoplasm By similarity UniProtKB P18925.

Miscellaneous

The active site is a redox-active disulfide bond By similarity. UniProtKB P18925

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
Direct protein sequencing
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 – 464464Dihydrolipoyl dehydrogenase
PRO_0000068036

Regions

Nucleotide binding36 – 449FAD By similarity UniProtKB P18925
Nucleotide binding184 – 1885NAD By similarity
Nucleotide binding269 – 2724NAD By similarity

Sites

Active site4431Proton acceptor By similarity UniProtKB P18925
Binding site531FAD By similarity
Binding site1191FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2071NAD By similarity
Binding site3111FAD By similarity
Binding site3191FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond44 ↔ 49Redox-active By similarity UniProtKB P18925

Sequences

Sequence LengthMass (Da)Tools
Q9I1L9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 52604A0708418434

FASTA46448,589
        10         20         30         40         50         60 
MSQILKTSLL IVGGGPGGYV AAIRAGQLGI PTVLVEGAAL GGTCLNVGCI PSKALIHAAE 

        70         80         90        100        110        120 
EYLKARHYAS RSALGIQVQA PSIDIARTVE WKDAIVDRLT SGVAALLKKH GVDVVQGWAR 

       130        140        150        160        170        180 
ILDGKSVAVE LAGGGSQRIE CEHLLLAAGS QSVELPILPL GGKVISSTEA LAPGSLPKRL 

       190        200        210        220        230        240 
VVVGGGYIGL ELGTAYRKLG VEVAVVEAQP RILPGYDEEL TKPVAQALRR LGVELYLGHS 

       250        260        270        280        290        300 
LLGPSENGVR VRDGAGEERE IAADQVLVAV GRKPRSEGWN LESLGLDMNG RAVKVDDQCR 

       310        320        330        340        350        360 
TSMRNVWAIG DLAGEPMLAH RAMAQGEMVA ELIAGKRRQF APVAIPAVCF TDPEVVVAGL 

       370        380        390        400        410        420 
SPEQAKDAGL DCLVASFPFA ANGRAMTLEA NEGFVRVVAR RDNHLVVGWQ AVGKAVSELS 

       430        440        450        460 
TAFAQSLEMG ARLEDIAGTI HAHPTLGEAV QEAALRALGH ALHI

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Biofouling in water treatment systems: effect of membrane properties on biofilm formation."
Liddor M.
Thesis (2005), Ben-Gurion University, Israel
Cited for: PROTEIN SEQUENCE OF 7-24; 54-64; 72-87; 99-108; 164-178; 199-211; 253-272; 305-336; 385-396 AND 415-456.
Strain: ATCC 33467 / type 1 smooth.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004091 Genomic DNA. Translation: AAG05638.1.
PIRF83365.
RefSeqNP_250940.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9I1L9.
SMRQ9I1L9. Positions 3-464.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA2250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID878470.
KEGGpae:PA2250.
PATRIC19838942. VBIPseAer58763_2351.

Organism-specific databases

PseudoCAPPA2250.

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276708.
KOK00382.
OMATIAWKDG.
ProtClustDBPRK05976.

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 nameDLDH1_PSEAE
AccessionPrimary (citable) accession number: Q9I1L9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 79 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents