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Reviewed, UniProtKB/Swiss-Prot P0A9P2 (DLDH_ECO57)

Last modified June 16, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
    Glycine cleavage system L protein
Gene names
Name: lpdA
Ordered Locus Names: Z0126, ECs0120
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as 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 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.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMAcetylation
Disulfide 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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

dihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 474473Dihydrolipoyl dehydrogenase
PRO_0000068028

Regions

Nucleotide binding36 – 4510FAD By similarity
Nucleotide binding182 – 1865NAD By similarity
Nucleotide binding270 – 2734NAD By similarity

Sites

Active site4451Proton acceptor By similarity
Binding site541FAD By similarity
Binding site1171FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2051NAD By similarity
Binding site2381NAD; via amide nitrogen By similarity
Binding site3131FAD By similarity
Binding site3211FAD; via amide nitrogen By similarity

Amino acid modifications

Modified residue2201N6-acetyllysine By similarity
Disulfide bond45 ↔ 50Redox-active By similarity

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Sequences

Sequence LengthMass (Da)Tools
P0A9P2-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: ED16149A3BDF333A

FASTA47450,688
        10         20         30         40         50         60 
MSTEIKTQVV VLGAGPAGYS AAFRCADLGL ETVIVERYNT LGGVCLNVGC IPSKALLHVA 

        70         80         90        100        110        120 
KVIEEAKALA EHGIVFGEPK TDIDKIRTWK EKVINQLTGG LAGMAKGRKV KVVNGLGKFT 

       130        140        150        160        170        180 
GANTLEVEGE NGKTVINFDN AIIAAGSRPI QLPFIPHEDP RIWDSTDALE LKEVPERLLV 

       190        200        210        220        230        240 
MGGGIIGLEM GTVYHALGSQ IDVVEMFDQV IPAADKDIVK VFTKRISKKF NLMLETKVTA 

       250        260        270        280        290        300 
VEAKEDGIYV TMEGKKAPAE PQRYDAVLVA IGRVPNGKNL DAGKAGVEVD DRGFIRVDKQ 

       310        320        330        340        350        360 
LRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVIAGKKH YFDPKVIPSI AYTEPEVAWV 

       370        380        390        400        410        420 
GLTEKEAKEK GISYETATFP WAASGRAIAS DCADGMTKLI FDKESHRVIG GAIVGTNGGE 

       430        440        450        460        470 
LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNPK AKKK

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References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

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Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG54420.1.
BA000007 Genomic DNA. Translation: BAB33543.1.
PIRH85494.
H90643.
RefSeqNP_285812.1.
NP_308147.1.

3D structure databases

HSSPHSSP built from PDB template 1OJT based on UniProtKB Q51225.
ModBaseSearch...

Genome annotation databases

GeneID913660.
956813.
GenomeReviewsGene locus Z0126 in contig AE005174_GR.
Gene locus ECs0120 in contig BA000007_GR.
KEGGece:Z0126.
ecs:ECs0120.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0A9P2.
OMAP0A9P2. MMDGLMA.

Enzyme and pathway databases

BioCycECOL83334:ECS0120-MON.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
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.
PR00945. HGRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDLDH_ECO57
AccessionPrimary (citable) accession number: P0A9P2
Secondary accession number(s): P00391
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 35 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents