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Reviewed, UniProtKB/Swiss-Prot P09623 (DLDH_PIG)

Last modified June 16, 2009. Version 90. 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, mitochondrial
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
Gene names
Name: DLD
Synonyms: LAD
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

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

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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.

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

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. Homodimer.

Subcellular location

Mitochondrion matrix.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

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

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Ontologies

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

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

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

Transit peptide1 – 3535Mitochondrion Ref.2
Chain36 – 509474Dihydrolipoyl dehydrogenase, mitochondrial
PRO_0000030298

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
Disulfide bond80 ↔ 85Redox-active By similarity

Experimental info

Sequence conflict95 – 973SHY → GHA AA sequence Ref.2
Sequence conflict3461K → R AA sequence Ref.2
Sequence conflict3511Y → A AA sequence Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P09623-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 38A0469FED071300

FASTA50954,185
        10         20         30         40         50         60 
MQSWSRVYCT LAKRGHFNRI AHGLQGVSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA 

        70         80         90        100        110        120 
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL 

       130        140        150        160        170        180 
EKMMEQKSNA VKALTGGIAH LFKQNKVVRV NGYGKITGKN QVTATKADGS TEVINTKNIL 

       190        200        210        220        230        240 
IATGSEVTPF PGITIDEDTV VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT 

       250        260        270        280        290        300 
AVELLGHVGG IGIDMEVSKN FQRILQKQGF KFKLNTKVIG ATKKSDGNID VSIEAASGGK 

       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 LGAHIIGPGA GEMINEAALA LEYGASCEDI 

       490        500 
ARVCHAHPTL SEAFREANLA ASFGKAINF

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References

[1]"Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases."
Otulakowski G., Robinson B.H.
J. Biol. Chem. 262:17313-17318(1987) [PubMed: 3693355] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase."
Williams C.H. Jr., Arscott L.D., Schulz G.E.
Proc. Natl. Acad. Sci. U.S.A. 79:2199-2201(1982) [PubMed: 6954534] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-89; 91-104; 317-331; 346-360; 388-417 AND 450-482.
Tissue: Heart.

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Cross-references

Sequence databases

J03489 mRNA. Translation: AAA31069.1.
PIRDEPGLP. A28448.
RefSeqNP_999227.1.
UniGeneSsc.224

3D structure databases

HSSPHSSP built from PDB template 1JEH based on UniProtKB P09624.
SMRP09623. Positions 37-509.
ModBaseSearch...

Genome annotation databases

GeneID397129.
KEGGssc:397129.

Phylogenomic databases

HOVERGENP09623.

Enzyme and pathway databases

BRENDA1.8.1.4. 249.

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_PIG
AccessionPrimary (citable) accession number: P09623
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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