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Q8CIZ7 (DLDH_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 60. 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
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 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. 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.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

Tyrosine phosphorylated 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
   Cellular componentMitochondrion
   DomainRedox-active center
Transit peptide
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMAcetylation
Disulfide bond
Phosphoprotein
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 peptide1 – 3535Mitochondrion By similarity
Chain36 – 509474Dihydrolipoyl dehydrogenase, mitochondrial
PRO_0000260226

Regions

Nucleotide binding71 – 8010FAD By similarity
Nucleotide binding183 – 1853FAD By similarity
Nucleotide binding220 – 2278NAD By similarity
Nucleotide binding361 – 3644FAD By similarity

Sites

Active site4871Proton acceptor By similarity
Binding site891FAD By similarity
Binding site1541FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2431NAD By similarity
Binding site2781NAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3141NAD; via amide nitrogen By similarity
Binding site3551FAD By similarity

Amino acid modifications

Modified residue1271N6-acetyllysine By similarity
Modified residue1431N6-acetyllysine By similarity
Modified residue4101N6-acetyllysine By similarity
Modified residue4171N6-acetyllysine By similarity
Disulfide bond80 ↔ 85Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CIZ7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: FADBCF01E42576AB

FASTA50954,131
        10         20         30         40         50         60 
MQSWSRVYCS LAKRGHFNRI SHGLQGVSSV PLRTYADQPI DADVTVIGSG PGGYVAAIKA 

        70         80         90        100        110        120 
AQLGFKTVCI EKNDTLGGTC LNVGCIPSKA LLNNSHYYHL AHGRDFASRG IELSEVRLNL 

       130        140        150        160        170        180 
EKMMEQKSSA VKALIGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS SQVIGTKNIL 

       190        200        210        220        230        240 
IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT 

       250        260        270        280        290        300 
AVEFLGHVGG IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKRSDGKID VSVEAASGGK 

       310        320        330        340        350        360 
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP 

       370        380        390        400        410        420 
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK 

       430        440        450        460        470        480 
FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI 

       490        500 
ARVCHAHPTL SEAFREANLA ASFGKPINF

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References

[1]"2D gel analysis of the proteomic adaptation of a mammalian cell line to oxidative stress reveals changes in the expression of metabolically relevant enzymes."
Keightley J.A., Shang L., Kinter M.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF539836 mRNA. Translation: AAN15202.1.
RefSeqNP_001233626.1. NM_001246697.1.

3D structure databases

HSSPHSSP built from PDB template 2F5Z based on UniProtKB P09622.
ProteinModelPortalQ8CIZ7.
SMRQ8CIZ7. Positions 36-509.
ModBaseSearch...

Proteomic databases

PRIDEQ8CIZ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689437.

Organism-specific databases

CTD1738.

Phylogenomic databases

HOVERGENHBG002290.

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_CRIGR
AccessionPrimary (citable) accession number: Q8CIZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2003
Last modified: March 6, 2013
This is version 60 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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