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O08749

- DLDH_MOUSE

UniProt

O08749 - DLDH_MOUSE

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Protein
Dihydrolipoyl dehydrogenase, mitochondrial
Gene
Dld
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Binds 1 FAD per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FAD By similarity
Binding sitei154 – 1541FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei243 – 2431NAD By similarity
Binding sitei278 – 2781NAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei314 – 3141NAD; via amide nitrogen By similarity
Binding sitei355 – 3551FAD By similarity
Active sitei487 – 4871Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi71 – 8010FAD By similarity
Nucleotide bindingi183 – 1853FAD By similarity
Nucleotide bindingi220 – 2278NAD By similarity
Nucleotide bindingi361 – 3644FAD By similarity

GO - Molecular functioni

  1. dihydrolipoyl dehydrogenase activity Source: MGI
  2. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. gastrulation Source: MGI
  3. mitochondrial electron transport, NADH to ubiquinone Source: MGI
  4. proteolysis Source: MGI
  5. regulation of membrane potential Source: MGI
  6. sperm capacitation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

ReactomeiREACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene namesi
Name:Dld
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:107450. Dld.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal matrix Source: MGI
  2. cilium Source: MGI
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: MGI
  5. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535Mitochondrion By similarity
Add
BLAST
Chaini36 – 509474Dihydrolipoyl dehydrogenase, mitochondrial
PRO_0000030297Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysine; alternate2 Publications
Modified residuei66 – 661N6-succinyllysine; alternate1 Publication
Disulfide bondi80 ↔ 85Redox-active By similarity
Modified residuei104 – 1041N6-acetyllysine; alternate1 Publication
Modified residuei104 – 1041N6-succinyllysine; alternate1 Publication
Modified residuei122 – 1221N6-acetyllysine; alternate1 Publication
Modified residuei122 – 1221N6-succinyllysine; alternate1 Publication
Modified residuei132 – 1321N6-acetyllysine; alternate1 Publication
Modified residuei132 – 1321N6-succinyllysine; alternate1 Publication
Modified residuei143 – 1431N6-acetyllysine; alternate1 Publication
Modified residuei143 – 1431N6-succinyllysine; alternate1 Publication
Modified residuei159 – 1591N6-succinyllysine1 Publication
Modified residuei166 – 1661N6-succinyllysine1 Publication
Modified residuei273 – 2731N6-succinyllysine1 Publication
Modified residuei277 – 2771N6-succinyllysine1 Publication
Modified residuei334 – 3341N6-acetyllysine; alternate1 Publication
Modified residuei334 – 3341N6-succinyllysine; alternate1 Publication
Modified residuei346 – 3461N6-acetyllysine1 Publication
Modified residuei410 – 4101N6-acetyllysine; alternate2 Publications
Modified residuei410 – 4101N6-succinyllysine; alternate1 Publication
Modified residuei417 – 4171N6-acetyllysine By similarity
Modified residuei420 – 4201N6-acetyllysine1 Publication
Modified residuei430 – 4301N6-succinyllysine1 Publication
Modified residuei505 – 5051N6-acetyllysine; alternate1 Publication
Modified residuei505 – 5051N6-succinyllysine; alternate1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiO08749.
PaxDbiO08749.
PRIDEiO08749.

2D gel databases

REPRODUCTION-2DPAGEO08749.
SWISS-2DPAGEO08749.

PTM databases

PhosphoSiteiO08749.

Expressioni

Gene expression databases

BgeeiO08749.
CleanExiMM_DLD.
GenevestigatoriO08749.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi199227. 1 interaction.
IntActiO08749. 9 interactions.
MINTiMINT-4124146.

Structurei

3D structure databases

ProteinModelPortaliO08749.
SMRiO08749. Positions 38-509.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
HOVERGENiHBG002290.
KOiK00382.
OMAiIWNSTDA.
OrthoDBiEOG77126S.
PhylomeDBiO08749.
TreeFamiTF300414.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. 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]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08749-1 [UniParc]FASTAAdd to Basket

« Hide

MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG    50
PGGYVAAIKS AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM 100
AHGKDFASRG IEIPEVRLNL EKMMEQKHSA VKALTGGIAH LFKQNKVVHV 150
NGFGKITGKN QVTATKADGS TQVIDTKNIL VATGSEVTPF PGITIDEDTI 200
VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG 250
IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK 300
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI 350
YAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA 400
WVGKSEEQLK EEGIEFKIGK FPFAANSRAK TNADTDGMVK ILGHKSTDRV 450
LGAHILGPGA GEMVNEAALA LEYGASCEDI ARVCHAHPTL SEAFREANLA 500
AAFGKPINF 509
Length:509
Mass (Da):54,272
Last modified:November 28, 2006 - v2
Checksum:i2C381852BAAD0441
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541Y → C in AAC53170. 1 Publication
Sequence conflicti144 – 1441Q → T in BAE22867. 1 Publication
Sequence conflicti149 – 1491H → L in BAE31961. 1 Publication
Sequence conflicti283 – 2831K → E in BAE40693. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS36428.1.
RefSeqiNP_031887.2. NM_007861.5.
UniGeneiMm.3131.
Mm.471230.

Genome annotation databases

EnsembliENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664.
GeneIDi13382.
KEGGimmu:13382.
UCSCiuc007nhg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS36428.1.
RefSeqi NP_031887.2. NM_007861.5.
UniGenei Mm.3131.
Mm.471230.

3D structure databases

ProteinModelPortali O08749.
SMRi O08749. Positions 38-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199227. 1 interaction.
IntActi O08749. 9 interactions.
MINTi MINT-4124146.

Chemistry

ChEMBLi CHEMBL2176826.

PTM databases

PhosphoSitei O08749.

2D gel databases

REPRODUCTION-2DPAGE O08749.
SWISS-2DPAGE O08749.

Proteomic databases

MaxQBi O08749.
PaxDbi O08749.
PRIDEi O08749.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000110857 ; ENSMUSP00000106481 ; ENSMUSG00000020664 .
GeneIDi 13382.
KEGGi mmu:13382.
UCSCi uc007nhg.2. mouse.

Organism-specific databases

CTDi 1738.
MGIi MGI:107450. Dld.

Phylogenomic databases

eggNOGi COG1249.
GeneTreei ENSGT00550000074844.
HOGENOMi HOG000276708.
HOVERGENi HBG002290.
KOi K00382.
OMAi IWNSTDA.
OrthoDBi EOG77126S.
PhylomeDBi O08749.
TreeFami TF300414.

Enzyme and pathway databases

Reactomei REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

NextBioi 283728.
PROi O08749.
SOURCEi Search...

Gene expression databases

Bgeei O08749.
CleanExi MM_DLD.
Genevestigatori O08749.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. 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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01350. lipoamide_DH. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiDLDH_MOUSE
AccessioniPrimary (citable) accession number: O08749
Secondary accession number(s): Q3TG55
, Q3U5W5, Q3UWP7, Q99LD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 28, 2006
Last modified: September 3, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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