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O05940 (DLDH_RHIEC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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
EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
ORF-E3
Gene names
Name:lpdA
Ordered Locus Names:RHE_CH01938
OrganismRhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP]
Taxonomic identifier347834 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

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
   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

   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 – 481481Dihydrolipoyl dehydrogenase
PRO_0000068041

Regions

Nucleotide binding34 – 429FAD By similarity
Nucleotide binding195 – 1995NAD By similarity
Nucleotide binding284 – 2874NAD By similarity

Sites

Active site4601Proton acceptor By similarity
Binding site511FAD By similarity
Binding site2181NAD By similarity
Binding site3261FAD By similarity
Binding site3341FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond42 ↔ 47Redox-active By similarity

Experimental info

Sequence conflict3021K → L in CAA72399. Ref.2
Sequence conflict306 – 3083GCV → RWL in CAA72399. Ref.2
Sequence conflict332 – 3332ML → IV in CAA72399. Ref.2
Sequence conflict3511L → V in CAA72399. Ref.2
Sequence conflict3871R → S in CAA72399. Ref.2
Sequence conflict4001G → R in CAA72399. Ref.2
Sequence conflict479 – 4813Missing in CAA72399. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O05940 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: 873F3ABC67179655

FASTA48150,956
        10         20         30         40         50         60 
MAESYDVIII GSGPGGYVAA IRASQLGLKT AIVEREHMGG ICLNWGCIPT KALLRSAEVL 

        70         80         90        100        110        120 
DHANHFKDFG LVLEGSVKPD AKAVVGRSRA VSARLNAGVG FLMKKNKIDI IWGEAKLTKP 

       130        140        150        160        170        180 
GEIVVGKSSK PVVEPQHPLP KNVKGEGTYT AKHIIIATGA RPRALPGIEP DGKLIWTYFE 

       190        200        210        220        230        240 
ALKPDALPKS LIVMGSGAIG IEFASFYRSM GVDVTVVEVM PTIMPVEDAE ITAIARKQLE 

       250        260        270        280        290        300 
KRGLKIFTSA KVTKVEKGAG SITAHVETSD GKVQQITADR MISAVGVQGN IENLGLEALG 

       310        320        330        340        350        360 
VKTDRGCVVA DGYGKTNVAG IYAIGDVAGP PMLAHKAEHE GVVCVEKIAG LPNVHPTDKG 

       370        380        390        400        410        420 
KVPGCTYCNP QVASVGLTEA KAKELGRDIR VGRFSFAANG KAIALGEDQG MVKVIFDKKT 

       430        440        450        460        470        480 
GELLGAHMVG AEVTELIQGF VVAMNLETTE EELMHTIFPH PTVSETMKEA VLDAYGRVLN 


A

« Hide

References

« Hide 'large scale' references
[1]"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons."
Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G.
Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed: 16505379] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFN 42 / ATCC 51251.
[2]"Cloning and transcriptional analysis of the lipA (lipoic acid synthetase) gene from Rhizobium etli."
Tate R., Riccio A., Iaccarino M., Patriarca E.J.
FEMS Microbiol. Lett. 149:165-172(1997) [PubMed: 9141657] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-481.
Strain: CE3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000133 Genomic DNA. Translation: ABC90724.1.
Y11708 Genomic DNA. Translation: CAA72399.1.
RefSeqYP_469451.1. NC_007761.1.

3D structure databases

ProteinModelPortalO05940.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3893976.
KEGGret:RHE_CH01938.
PATRIC23085360. VBIRhiEtl108884_2336.

Organism-specific databases

CMRSearch...

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.
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 nameDLDH_RHIEC
AccessionPrimary (citable) accession number: O05940
Secondary accession number(s): Q2K8W2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 21, 2011
Last modified: January 25, 2012
This is version 82 of the entry and version 2 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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