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P0A0E6 (DLDH_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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
EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of pyruvate complex
Membrane-bound ribosome protein complex 50 kDa subunit
Gene names
Name:pdhD
Ordered Locus Names:SAV1096
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes 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 Potential. Membrane; Peripheral membrane protein.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

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

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
Membrane
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete 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

membrane

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 – 468468Dihydrolipoyl dehydrogenase
PRO_0000068045

Regions

Nucleotide binding39 – 479FAD By similarity
Nucleotide binding183 – 1875NAD By similarity
Nucleotide binding271 – 2744NAD By similarity

Sites

Active site4461Proton acceptor By similarity
Binding site561FAD By similarity
Binding site1191FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2061NAD By similarity
Binding site3141FAD By similarity
Binding site3221FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond47 ↔ 52Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A0E6 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 7B061FE2C39ED2D9

FASTA46849,451
        10         20         30         40         50         60 
MVVGDFPIET DTIVIGAGPG GYVAAIRAAQ LGQKVTIVEK GNLGGVCLNV GCIPSKALLH 

        70         80         90        100        110        120 
ASHRFVEAQH SENLGVIAES VSLNFQKVQE FKSSVVNKLT GGVEGLLKGN KVNIVKGEAY 

       130        140        150        160        170        180 
FVDNNSLRVM DEKSAQTYNF KNAIIATGSR PIEIPNFKFG KRVIDSTGAL NLQEVPGKLV 

       190        200        210        220        230        240 
VVGGGYIGSE LGTAFANFGS EVTILEGAKD ILGGFEKQMT QPVKKGMKEK GVEIVTEAMA 

       250        260        270        280        290        300 
KSAEETDNGV KVTYEAKGEE KTIEADYVLV TVGRRPNTDE LGLEELGVKF ADRGLLEVDK 

       310        320        330        340        350        360 
QSRTSISNIY AIGDIVPGLP LAHKASYEAK VAAEAIDGQA AEVDYIGMPA VCFTEPELAT 

       370        380        390        400        410        420 
VGYSEAQAKE EGLAIKASKF PYAANGRALS LDDTNGFVKL ITLKEDDTLI GAQVVGTGAS 

       430        440        450        460 
DIISELGLAI EAGMNAEDIA LTIHAHPTLG EMTMEAAEKA IGYPIHTM

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000017 Genomic DNA. Translation: BAB57258.1.
RefSeqNP_371620.1. NC_002758.2.

3D structure databases

ProteinModelPortalP0A0E6.
SMRP0A0E6. Positions 8-461.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0A0E6.

2D gel databases

World-2DPAGE0002:P0A0E6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000007013; EBSTAP00000006831; EBSTAG00000007012.
GeneID1121073.
GenomeReviewsGene locus SAV1096 in contig BA000017_GR.
KEGGsav:SAV1096.
PATRIC19562891. VBIStaAur52173_1124.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1249.
GeneTreeEBGT00050000023767.
HOGENOMHBG515043.
OMAPFIPEDP.
PhylomeDBP0A0E6.
ProtClustDBPRK06416.

Enzyme and pathway databases

BioCycSAUR158878:SAV1096-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. 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 nameDLDH_STAAM
AccessionPrimary (citable) accession number: P0A0E6
Secondary accession number(s): Q59822
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 57 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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