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P90597 (DLDH_TRYCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:LPD
OrganismTrypanosoma cruzi
Taxonomic identifier5693 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Schizotrypanum

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

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
   Coding sequence diversityPolymorphism
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
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: InterPro

   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 – 477477Dihydrolipoyl dehydrogenase
PRO_0000068009

Regions

Nucleotide binding41 – 5010FAD By similarity
Nucleotide binding153 – 1553FAD By similarity
Nucleotide binding190 – 1978NAD By similarity
Nucleotide binding330 – 3334FAD By similarity

Sites

Active site4561Proton acceptor By similarity
Binding site591FAD By similarity
Binding site1241FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2131NAD By similarity
Binding site2481NAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2821NAD; via amide nitrogen By similarity
Binding site3231FAD By similarity

Amino acid modifications

Disulfide bond50 ↔ 55Redox-active By similarity

Natural variations

Natural variant671V → L in allele 1 and allele 2.
Natural variant1441F → L in allele 1 and allele 2.
Natural variant2081K → E in allele 1 and allele 2.
Natural variant2561D → G in allele 1.
Natural variant2681K → R in allele 2.
Natural variant3761E → D in allele 1 and allele 2.
Natural variant4741T → S in allele 1 and allele 2.

Secondary structure

1 ............................................................................... 477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P90597 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 3A02415DFAB7E0EA

FASTA47750,491
        10         20         30         40         50         60 
MFRRCAVKLN PYDVVVIGGG PGGYVASIKA AQLGMKTACV EKRGALGGTC LNVGCIPSKA 

        70         80         90        100        110        120 
LLHATHVYHD AHANFARYGL MGGEGVTMDS AKMQQQKERA VKGLTGGVEY LFKKNKVTYY 

       130        140        150        160        170        180 
KGEGSFETAH SIRVNGLDGK QEMFETKKTI IATGSEPTEL PFLPFDEKVV LSSTGALALP 

       190        200        210        220        230        240 
RVPKTMVVIG GGVIGLELGS VWARLGAKVT VVEFAPRCAP TLDEDVTNAL VGALAKNEKM 

       250        260        270        280        290        300 
KFMTSTKVVG GTNNGDSVSL EVEGKNGKRE TVTCEALLVS VGRRPFTGGL GLDKINVAKN 

       310        320        330        340        350        360 
ERGFVKIGDH FETSIPDVYA IGDVVDKGPM LAHKAEDEGV ACAEILAGKP GHVNYGVIPA 

       370        380        390        400        410        420 
VIYTMPEVAS VGKSEEELKK EGVAYKVGKF PFNANSRAKA VSTEDGFVKV LVDKATDRIL 

       430        440        450        460        470 
GVHIVCTTAG ELIGEACLAM EYGASSEDVG RTCHAHPTMS EALKEACMAL VAKTINF

« Hide

References

[1]"Cloning, sequencing and functional expression of dihydrolipoamide dehydrogenase from the human pathogen Trypanosoma cruzi."
Schoeneck R., Billaut-Mulot O., Numrich P., Ouaissi M.A., Krauth-Siegel R.L.
Eur. J. Biochem. 243:739-747(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: Y.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X89112 mRNA. Translation: CAA61483.1.
Y11262 Genomic DNA. Translation: CAA72132.1.
Y11261 Genomic DNA. Translation: CAA72131.1.
PIRS13863.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QAEX-ray1.90A/B10-477[»]
ProteinModelPortalP90597.
SMRP90597. Positions 10-477.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP90597.

Entry information

Entry nameDLDH_TRYCR
AccessionPrimary (citable) accession number: P90597
Secondary accession number(s): P90598, P90599
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
Last modified: April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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