Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O08749

- DLDH_MOUSE

UniProt

O08749 - DLDH_MOUSE

Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

Dld

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 891FADBy similarity
    Binding sitei154 – 1541FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei243 – 2431NADBy similarity
    Binding sitei278 – 2781NAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei314 – 3141NAD; via amide nitrogenBy similarity
    Binding sitei355 – 3551FADBy similarity
    Active sitei487 – 4871Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi71 – 8010FADBy similarity
    Nucleotide bindingi183 – 1853FADBy similarity
    Nucleotide bindingi220 – 2278NADBy similarity
    Nucleotide bindingi361 – 3644FADBy 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

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535MitochondrionBy similarityAdd
    BLAST
    Chaini36 – 509474Dihydrolipoyl dehydrogenase, mitochondrialPRO_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-activeBy 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-acetyllysineBy 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.2 Publications
    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.By similarity

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliO08749.
    SMRiO08749. Positions 38-509.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541Y → C in AAC53170. (PubMed:9169128)Curated
    Sequence conflicti144 – 1441Q → T in BAE22867. (PubMed:16141072)Curated
    Sequence conflicti149 – 1491H → L in BAE31961. (PubMed:16141072)Curated
    Sequence conflicti283 – 2831K → E in BAE40693. (PubMed:16141072)Curated

    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

    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: October 1, 2014
    This is version 129 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