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Q9I3D1 (DLDH2_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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:
Dihydrolipoamide dehydrogenase
EC=1.8.1.4
Alternative name(s):
E3 component of 2-oxoglutarate dehydrogenase complex
Glycine oxidation system L-factor
LPD-GLC
Gene names
Name:lpdG
Ordered Locus Names:PA1587
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Also acts in the glycine cleavage system 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 – 478478Dihydrolipoamide dehydrogenase
PRO_0000287805

Regions

Nucleotide binding34 – 4916FAD By similarity
Nucleotide binding188 – 1925NAD By similarity
Nucleotide binding276 – 2794NAD By similarity

Sites

Active site4511Proton acceptor By similarity
Binding site581FAD By similarity
Binding site1221FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2111NAD By similarity
Binding site2451NAD; via amide nitrogen By similarity
Binding site3191FAD By similarity
Binding site3271FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond49 ↔ 54Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I3D1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A93C7B03B3C7470F

FASTA47850,165
        10         20         30         40         50         60 
MSQKFDVVVI GAGPGGYVAA IRAAQLGLKT ACIEKYIGKE GKVALGGTCL NVGCIPSKAL 

        70         80         90        100        110        120 
LDSSYKYHEA KEAFKVHGIE AKGVTIDVPA MVARKANIVK NLTGGIATLF KANGVTSFEG 

       130        140        150        160        170        180 
HGKLLANKQV EVTGLDGKTQ VLEAENVIIA SGSRPVEIPP APLTDDIIVD STGALEFQAV 

       190        200        210        220        230        240 
PKKLGVIGAG VIGLELGSVW ARLGAEVTVL EALDKFLPAA DEQIAKEALK VLTKQGLNIR 

       250        260        270        280        290        300 
LGARVTASEV KKKQVTVTFT DANGEQKETF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF 

       310        320        330        340        350        360 
IYVDDHCKTS VPGVFAIGDV VRGAMLAHKA SEEGVMVAER IAGHKAQMNY DLIPSVIYTH 

       370        380        390        400        410        420 
PEIAWVGKTE QTLKAEGVEV NVGTFPFAAS GRAMAANDTT GLVKVIADAK TDRVLGVHVI 

       430        440        450        460        470 
GPSAAELVQQ GAIGMEFGTS AEDLGMMVFS HPTLSEALHE AALAVNGHAI HIANRKKR

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004091 Genomic DNA. Translation: AAG04976.1.
PIRA83449.
RefSeqNP_250278.1. NC_002516.2.

3D structure databases

HSSPHSSP built from PDB template 1LPF based on UniProtKB P14218.
ProteinModelPortalQ9I3D1.
SMRQ9I3D1. Positions 2-473.
ModBaseSearch...

Proteomic databases

PRIDEQ9I3D1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID882090.
GenomeReviewsGene locus PA1587 in contig AE004091_GR.
KEGGpae:PA1587.
PATRIC19837520. VBIPseAer58763_1646.

Organism-specific databases

PseudoCAPPA1587.

Phylogenomic databases

HOGENOMHBG515043.
OMAVDDHCAT.
ProtClustDBPRK06467.

Enzyme and pathway databases

BioCycPAER208964:PA1587-MONOMER.

Family and domain databases

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]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KOK00382.
PANTHERPTHR22912:SF20. Lipoamide_DH. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 2 hits.
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 nameDLDH2_PSEAE
AccessionPrimary (citable) accession number: Q9I3D1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 70 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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