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Q811C4 (DLDH_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 55. 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, mitochondrial
EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene names
Name:DLD
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length479 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction. Ref.1 UniProtKB P09622

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. UniProtKB P09622

Cofactor

Binds 1 FAD per subunit By similarity. UniProtKB P31023

Subunit structure

Homodimer. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds By similarity. UniProtKB P09622

Subcellular location

Mitochondrion matrix By similarity UniProtKB P09622.

Post-translational modification

Tyrosine phosphorylated. Ref.1

Miscellaneous

The active site is a redox-active disulfide bond By similarity. UniProtKB P09622

Sequence similarities

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

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainRedox-active center
Transit peptide
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrial matrix

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

Transit peptide‹1 – 19›19Mitochondrion Ref.1
Chain20 – ›479›460Dihydrolipoyl dehydrogenase, mitochondrial Ref.1
PRO_5000070424

Regions

Nucleotide binding55 – 6410FAD By similarity UniProtKB P09622
Nucleotide binding167 – 1693FAD By similarity UniProtKB P09622
Nucleotide binding204 – 2118NAD By similarity UniProtKB P09622
Nucleotide binding345 – 3484FAD By similarity UniProtKB P09622

Sites

Active site4711Proton acceptor By similarity UniProtKB P09624
Binding site731FAD By similarity UniProtKB P09622
Binding site1381FAD; via amide nitrogen and carbonyl oxygen By similarity UniProtKB P09622
Binding site2271NAD By similarity UniProtKB P09622
Binding site2621NAD; via amide nitrogen and carbonyl oxygen By similarity UniProtKB P09622
Binding site2981NAD; via amide nitrogen By similarity UniProtKB P09622
Binding site3391FAD By similarity UniProtKB P09622

Amino acid modifications

Modified residue1111N6-acetyllysine By similarity UniProtKB O08749
Modified residue1271N6-acetyllysine By similarity UniProtKB P09622
Modified residue3941N6-acetyllysine By similarity UniProtKB P09622
Modified residue4011N6-acetyllysine By similarity UniProtKB P09622
Disulfide bond64 ↔ 69Redox-active By similarity UniProtKB P09622

Experimental info

Non-terminal residue11
Non-terminal residue4791

Sequences

Sequence LengthMass (Da)Tools
Q811C4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1F2EA60777B3DCE4

FASTA47950,723
        10         20         30         40         50         60 
FNRXSPGLQG VSSVPLRTYA DQPIDADVTV IGSGPGGYVA AIKAAQLGFK TVCIEKNETL 

        70         80         90        100        110        120 
GGTCLNVGCI PSKALLNNSH YYHLAHGKDF ASRGIELSEV RLNLEKMMEQ KSSAVKALTG 

       130        140        150        160        170        180 
GIAHLFKQNK VVHVNGFGNI TGKNQVTATK ADGSSQVIGT KNILIATGSE VTPFPGITID 

       190        200        210        220        230        240 
EDTIVSSTGA LSLKKVPEKL VVIGAGVIGV ELGSVWQRLG AEVTAVEFLG HVGGIGIDME 

       250        260        270        280        290        300 
ISKKFQRILQ KQGFKFKLNP KVPGATKRSD GKIDVSVEAA PGGKAEVIPC DVLLVCIGRR 

       310        320        330        340        350        360 
PFTQNLGLEE LGIELDPRGR IPVNTRFQTK IPNIYAIGDV VAGPMLAHKA EDEGIICVEG 

       370        380        390        400        410        420 
MAGGAVHIDY NCVPSVIYTH PEVAWVGKSE EQLKEEGIEY KVGKFPFAAN SRAKTNADTD 

       430        440        450        460        470 
GMVKILGQKS TDRVLGAHIL GPGAGEMVNE AALALEYGAS CEDIARVCHA HPTLSEAFR

« Hide

References

[1]"Novel tyrosine-phosphorylated post-pyruvate metabolic enzyme, dihydrolipoamide dehydrogenase, involved in capacitation of hamster spermatozoa."
Mitra K., Shivaji S.
Biol. Reprod. 70:887-899(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-51, FUNCTION, PHOSPHORYLATION.
Tissue: Sperm and Testis.
[2]"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ538298 mRNA. Translation: CAD61860.1.

3D structure databases

HSSPHSSP built from PDB template 1JEH based on UniProtKB P09624.
ProteinModelPortalQ811C4.
ModBaseSearch...

Proteomic databases

PRIDEQ811C4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG002290.

Enzyme and pathway databases

BRENDA1.8.1.4. 3239.

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...

Entry information

Entry nameDLDH_MESAU
AccessionPrimary (citable) accession number: Q811C4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 1, 2003
Last modified: March 6, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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