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Q54EW8 (DLDH_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase, mitochondrial

EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
Glycine cleavage system L protein
Gene names
Name:lpd
Synonyms:bkdD, dld, odhC, pdhD
ORF Names:DDB_G0291648
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Subcellular location

Mitochondrion matrix Potential.

Miscellaneous

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

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
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-serine biosynthetic process

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

acetyl-CoA biosynthetic process from pyruvate

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycine catabolic process

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

isoleucine catabolic process

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

leucine catabolic process

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

valine catabolic process

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

   Cellular_componentmitochondrial matrix

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

mitochondrial pyruvate dehydrogenase complex

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

phagocytic vesicle

Inferred from direct assay PubMed 19482547. Source: dictyBase

   Molecular_functiondihydrolipoyl dehydrogenase activity

Inferred from sequence or structural similarity Ref.2. Source: dictyBase

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 – 2525Mitochondrion Potential
Chain26 – 488463Dihydrolipoyl dehydrogenase, mitochondrial
PRO_0000327450

Regions

Nucleotide binding52 – 6110FAD By similarity
Nucleotide binding163 – 1653FAD By similarity
Nucleotide binding200 – 2078NAD By similarity
Nucleotide binding341 – 3444FAD By similarity

Sites

Active site4671Proton acceptor By similarity
Binding site701FAD By similarity
Binding site1341FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2231NAD By similarity
Binding site2571NAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2941NAD; via amide nitrogen By similarity
Binding site3351FAD By similarity

Amino acid modifications

Disulfide bond61 ↔ 66Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q54EW8 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: A7DD67E8F7707783

FASTA48851,794
        10         20         30         40         50         60 
MLRINRISNL RTFGQRFFST EQQDVVVIGG GPGGYVAGIK AGQLGMKVTV VEKRGKLGGT 

        70         80         90        100        110        120 
CLNVGCIPSK ALLNASHLYE EATTKMSKYG VKCSGVELDL GAMMQYKDKS VSGLTSGIEG 

       130        140        150        160        170        180 
LFKKNKVKYD KGFGKITGPN TVEVTLNDGS VKTIETKNIV IATGSEVTSL PNVNIDEESI 

       190        200        210        220        230        240 
ISSTGALALK SVPKKLIVIG GGVIGLELGS VWSRLGSETT VVEFTNRIAA GADGEVAKKF 

       250        260        270        280        290        300 
QKSLEKQHMK FHLETKVTSV VKKSDGKVTV TVEQVGAGGF TGTLEADAVL VSVGRRPNTS 

       310        320        330        340        350        360 
GLGLESVGIP TDKAGRVEVG DHFNTKVPSI FAIGDAIRGP MLAHKAEEEG IAIIEQIHNG 

       370        380        390        400        410        420 
GGHVNYGAIP SIIYTHPEVA WVGKTEEELQ KEGIQYNIGR FPFVANSRAK TNDDVEGFVK 

       430        440        450        460        470        480 
FLAAKDSDRV LGAHIMGTNA GELIGECVLA MEYGASCEDI ARTCHGHPTL SEAVKEAAMD 


AYDKPIHM 

« Hide

References

« Hide 'large scale' references
[1]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[2]"A first glimpse into the pattern and scale of gene transfer in Apicomplexa."
Huang J., Mullapudi N., Sicheritz-Ponten T., Kissinger J.C.
Int. J. Parasitol. 34:265-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-357.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000177 Genomic DNA. Translation: EAL61808.1.
AY466389 Genomic DNA. Translation: AAS47709.1.

3D structure databases

ProteinModelPortalQ54EW8.
SMRQ54EW8. Positions 20-488.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0216232.

Proteomic databases

PRIDEQ54EW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0216232; DDB0216232; DDB_G0291648.
KEGGddi:DDB_G0291648.

Organism-specific databases

dictyBaseDDB_G0291648. lpd.

Phylogenomic databases

eggNOGCOG1249.
KOK00382.
OMAIDSEYRT.
PhylomeDBQ54EW8.
ProtClustDBCLSZ2429541.

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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ54EW8.

Entry information

Entry nameDLDH_DICDI
AccessionPrimary (citable) accession number: Q54EW8
Secondary accession number(s): Q6S4V6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase