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O08749 (DLDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. 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
Gene names
Name:Dld
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
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.

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.

Post-translational modification

Acetylation of Lys-127 is observed in liver mitochondria from fasted mice but not from fed mice.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion By similarity
Chain36 – 509474Dihydrolipoyl dehydrogenase, mitochondrial
PRO_0000030297

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 residue661N6-acetyllysine; alternate Ref.5 Ref.6
Modified residue661N6-succinyllysine; alternate Ref.5
Modified residue1041N6-acetyllysine; alternate Ref.6
Modified residue1041N6-succinyllysine; alternate Ref.5
Modified residue1221N6-acetyllysine; alternate Ref.6
Modified residue1221N6-succinyllysine; alternate Ref.5
Modified residue1321N6-acetyllysine; alternate Ref.6
Modified residue1321N6-succinyllysine; alternate Ref.5
Modified residue1431N6-acetyllysine; alternate Ref.6
Modified residue1431N6-succinyllysine; alternate Ref.5
Modified residue1591N6-succinyllysine Ref.5
Modified residue1661N6-succinyllysine Ref.5
Modified residue2731N6-succinyllysine Ref.5
Modified residue2771N6-succinyllysine Ref.5
Modified residue3341N6-acetyllysine; alternate Ref.6
Modified residue3341N6-succinyllysine; alternate Ref.5
Modified residue3461N6-acetyllysine Ref.6
Modified residue4101N6-acetyllysine; alternate Ref.5 Ref.6
Modified residue4101N6-succinyllysine; alternate Ref.5
Modified residue4171N6-acetyllysine By similarity
Modified residue4201N6-acetyllysine Ref.6
Modified residue4301N6-succinyllysine Ref.5
Modified residue5051N6-acetyllysine; alternate Ref.6
Modified residue5051N6-succinyllysine; alternate Ref.5
Disulfide bond80 ↔ 85Redox-active By similarity

Experimental info

Sequence conflict541Y → C in AAC53170. Ref.1
Sequence conflict1441Q → T in BAE22867. Ref.2
Sequence conflict1491H → L in BAE31961. Ref.2
Sequence conflict2831K → E in BAE40693. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O08749 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 2C381852BAAD0441

FASTA50954,272
        10         20         30         40         50         60 
MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG PGGYVAAIKS 

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

       130        140        150        160        170        180 
EKMMEQKHSA VKALTGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS TQVIDTKNIL 

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

       250        260        270        280        290        300 
AVEFLGHVGG IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK 

       310        320        330        340        350        360 
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI YAIGDVVAGP 

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

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

       490        500 
ARVCHAHPTL SEAFREANLA AAFGKPINF 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the mouse dihydrolipoamide dehydrogenase (Dld) gene: genomic structure, promoter sequence, and chromosomal localization."
Johnson M., Yang H.S., Johanning G.L., Patel M.S.
Genomics 41:320-326(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: DBA/2J.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow and Heart.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary tumor.
[4]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 73-89; 216-259; 289-334; 316-334; 347-365; 421-428 AND 483-509, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-410, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122; LYS-132; LYS-143; LYS-159; LYS-166; LYS-273; LYS-277; LYS-334; LYS-410; LYS-430 AND LYS-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122; LYS-132; LYS-143; LYS-334; LYS-346; LYS-410; LYS-420 AND LYS-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73445 mRNA. Translation: AAC53170.1.
AK117104 mRNA. Translation: BAE43405.1.
AK136193 mRNA. Translation: BAE22867.1.
AK153399 mRNA. Translation: BAE31961.1.
AK168875 mRNA. Translation: BAE40693.1.
BC003368 mRNA. Translation: AAH03368.1.
RefSeqNP_031887.2. NM_007861.5.
UniGeneMm.3131.
Mm.471230.

3D structure databases

ProteinModelPortalO08749.
SMRO08749. Positions 38-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199227. 1 interaction.
IntActO08749. 9 interactions.
MINTMINT-4124146.

Chemistry

ChEMBLCHEMBL2176826.

PTM databases

PhosphoSiteO08749.

2D gel databases

REPRODUCTION-2DPAGEO08749.
SWISS-2DPAGEO08749.

Proteomic databases

PaxDbO08749.
PRIDEO08749.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664.
GeneID13382.
KEGGmmu:13382.
UCSCuc007nhg.2. mouse.

Organism-specific databases

CTD1738.
MGIMGI:107450. Dld.

Phylogenomic databases

eggNOGCOG1249.
GeneTreeENSGT00550000074844.
HOGENOMHOG000276708.
HOVERGENHBG002290.
KOK00382.
OMAIDSEYRT.
OrthoDBEOG77126S.
PhylomeDBO08749.
TreeFamTF300414.

Gene expression databases

BgeeO08749.
CleanExMM_DLD.
GenevestigatorO08749.

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

NextBio283728.
PROO08749.
SOURCESearch...

Entry information

Entry nameDLDH_MOUSE
AccessionPrimary (citable) accession number: O08749
Secondary accession number(s): Q3TG55 expand/collapse secondary AC list , Q3U5W5, Q3UWP7, Q99LD3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 125 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot