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UniProtKB/Swiss-Prot entry O08749


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DLDH_MOUSE
Primary accession number O08749
Secondary accession numbers Q3TG55 Q3U5W5 Q3UWP7 Q99LD3
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on November 28, 2006 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 78)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase, mitochondrial [Precursor]
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
Gene name
Name: Dld
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=DBA/2J;
DOI=10.1006/geno.1997.4670; PubMed=9169128 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson M., Yang H.S., Johanning G.L., Patel M.S.;
"Characterization of the mouse dihydrolipoamide dehydrogenase (Dld) gene: genomic structure, promoter sequence, and chromosomal localization.";
Genomics 41:320-326(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Bone marrow, and Heart;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 73-89; 216-259; 289-300; 316-334; 347-365; 421-428 AND 483-509, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 301-334 AND 483-495, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
Comments
  • FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes.
  • CATALYTIC ACTIVITY: Protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH.
  • COFACTOR: Binds 1 FAD per subunit (By similarity).
  • SUBUNIT: 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.
  • PTM: Acetylation of Lys-127 is observed in liver mitochondria from fasted mice but not from fed mice.
  • MISCELLANEOUS: The active site is a redox-active disulfide bond.
  • SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U73445; AAC53170.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK117104; BAE43405.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK136193; BAE22867.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK153399; BAE31961.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK168875; BAE40693.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003368; AAH03368.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_031887.2; -.
UniGene Mm.3131
3D structure databases
HSSP P31023; 1DXL. [HSSP ENTRY / PDB]
SMR O08749; 37-509.
ModBase O08749.
PTM databases
PhosphoSite O08749; -.
2D gel databases
SWISS-2DPAGE O08749; -.
REPRODUCTION-2DPAGE O08749; -.
Organism-specific databases
MGI MGI:107450; Dld.
Gene expression databases
ArrayExpress O08749; -.
CleanEx MM_DLD; -.
GermOnline ENSMUSG00000020664; Mus musculus.
Ontologies
GO
GO:0043159; Cellular component: acrosomal matrix (inferred from direct assay from MGI).
GO:0019861; Cellular component: flagellum (inferred from direct assay from MGI).
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004148; Molecular function: dihydrolipoyl dehydrogenase activity (inferred from mutant phenotype from MGI).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0007369; Biological process: gastrulation (inferred from mutant phenotype from MGI).
GO:0006120; Biological process: mitochondrial electron transport, NADH to ubiquinone (inferred from mutant phenotype from MGI).
GO:0006508; Biological process: proteolysis (inferred from direct assay from MGI).
GO:0042391; Biological process: regulation of membrane potential (inferred from mutant phenotype from MGI).
GO:0048240; Biological process: sperm capacitation (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR006258; Lipoamide_DHase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
PANTHER PTHR22912:SF20; Lipoamide_DH; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01350; lipoamide_DH; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
Proteomics databases
PRIDE O08749; -.
Genome annotation databases
Ensembl ENSMUSG00000020664; Mus musculus. [Contig view]
GeneID 13382; -.
KEGG mmu:13382; -.
NMPDR fig|10090.3.peg.26069; -.
Phylogenomic databases
HOVERGEN O08749; -.
Other
NextBio 283728; -.
SOURCE Dld; Mus musculus.
ProtoNet O08749.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    35  35     Mitochondrion (By similarity). 
CHAIN   36   509  474     Dihydrolipoyl dehydrogenase, mitochondrial. PRO_0000030297
NP_BIND   71    80  10     FAD (By similarity). 
NP_BIND   183   185  3     FAD (By similarity). 
NP_BIND   220   227  8     NAD (By similarity). 
NP_BIND   361   364  4     FAD (By similarity). 
ACT_SITE   487   487        Proton acceptor (By similarity). 
BINDING   89    89        FAD (By similarity). 
BINDING   154   154        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   243   243        NAD (By similarity). 
BINDING   278   278        NAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   314   314        NAD; via amide nitrogen (By similarity). 
BINDING   355   355        FAD (By similarity). 
MOD_RES   127   127        N6-acetyllysine. 
DISULFID   80    85        Redox-active (By similarity). 
CONFLICT   54    54        Y -> C (in Ref. 1; AAC53170). 
CONFLICT   144   144        Q -> T (in Ref. 2; BAE22867). 
CONFLICT   149   149        H -> L (in Ref. 2; BAE31961). 
CONFLICT   283   283        K -> E (in Ref. 2; BAE40693). 
Sequence information
Length: 509 AA [This is the length of the unprocessed precursor] Molecular weight: 54272 Da [This is the MW of the unprocessed precursor] CRC64: 2C381852BAAD0441 [This is a checksum on the sequence]
        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 

O08749 in FASTA format

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