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Q6P6R2

- DLDH_RAT

UniProt

Q6P6R2 - DLDH_RAT

Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

Dld

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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 By similarity.By similarity

    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: RGD
    2. flavin adenine dinucleotide binding Source: RGD
    3. lipoamide binding Source: RGD
    4. NAD binding Source: RGD

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: RGD
    2. acetyl-CoA biosynthetic process from pyruvate Source: RGD
    3. aging Source: RGD
    4. cell redox homeostasis Source: InterPro
    5. dihydrolipoamide metabolic process Source: RGD
    6. lipoate metabolic process Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    ReactomeiREACT_203088. Pyruvate metabolism.
    REACT_216424. Citric acid cycle (TCA cycle).
    REACT_220761. Lysine catabolism.
    REACT_221218. Branched-chain amino acid catabolism.
    SABIO-RKQ6P6R2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4)
    Alternative name(s):
    Dihydrolipoamide dehydrogenase
    Gene namesi
    Name:Dld
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi735073. Dld.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: RGD
    3. oxoglutarate dehydrogenase complex Source: RGD
    4. pyruvate dehydrogenase complex Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535MitochondrionBy similarityAdd
    BLAST
    Chaini36 – 509474Dihydrolipoyl dehydrogenase, mitochondrialPRO_0000260228Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
    Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
    Disulfide bondi80 ↔ 85Redox-activeBy similarity
    Modified residuei104 – 1041N6-acetyllysine; alternateBy similarity
    Modified residuei104 – 1041N6-succinyllysine; alternateBy similarity
    Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
    Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
    Modified residuei132 – 1321N6-acetyllysine; alternateBy similarity
    Modified residuei132 – 1321N6-succinyllysine; alternateBy similarity
    Modified residuei143 – 1431N6-acetyllysine; alternateBy similarity
    Modified residuei143 – 1431N6-succinyllysine; alternateBy similarity
    Modified residuei159 – 1591N6-succinyllysineBy similarity
    Modified residuei273 – 2731N6-succinyllysineBy similarity
    Modified residuei277 – 2771N6-succinyllysineBy similarity
    Modified residuei346 – 3461N6-acetyllysineBy similarity
    Modified residuei410 – 4101N6-acetyllysine; alternateBy similarity
    Modified residuei410 – 4101N6-succinyllysine; alternateBy similarity
    Modified residuei417 – 4171N6-acetyllysineBy similarity
    Modified residuei420 – 4201N6-acetyllysineBy similarity
    Modified residuei430 – 4301N6-succinyllysineBy similarity
    Modified residuei505 – 5051N6-acetyllysine; alternateBy similarity
    Modified residuei505 – 5051N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    Tyrosine phosphorylated.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiQ6P6R2.
    PRIDEiQ6P6R2.

    PTM databases

    PhosphoSiteiQ6P6R2.

    Expressioni

    Gene expression databases

    GenevestigatoriQ6P6R2.

    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

    IntActiQ6P6R2. 1 interaction.
    MINTiMINT-1775384.
    STRINGi10116.ENSRNOP00000008980.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6P6R2.
    SMRiQ6P6R2. Positions 37-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG1249.
    GeneTreeiENSGT00550000074844.
    HOGENOMiHOG000276708.
    HOVERGENiHBG002290.
    KOiK00382.
    OMAiRMERGFV.
    OrthoDBiEOG77126S.
    PhylomeDBiQ6P6R2.
    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.

    Q6P6R2-1 [UniParc]FASTAAdd to Basket

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    MQSWSRVYCS LAKKGHFNRL SHGLQGASSV PLRTYSDQPI DADVTVIGSG    50
    PGGYVAAIKA AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHL 100
    AHGKDFASRG IEIPEVRLNL EKMMEQKRSA VKALTGGIAH LFKQNKVVHV 150
    NGFGKITGKN QVTATTADGS TQVIGTKNIL IATGSEVTPF PGITIDEDTI 200
    VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG 250
    IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK 300
    AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN TRFQTKIPNI 350
    FAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA 400
    WVGKSEEQLK EEGVEFKVGK FPFAANSRAK TNADTDGMVK ILGHKSTDRI 450
    LGAHILGPGA GEMVNEAALA LEYGASCEDV ARVCHAHPTL SEAFREANLA 500
    ASFGKPINF 509
    Length:509
    Mass (Da):54,038
    Last modified:July 5, 2004 - v1
    Checksum:i854802DBFE36573A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC062069 mRNA. Translation: AAH62069.1.
    RefSeqiNP_955417.1. NM_199385.2.
    UniGeneiRn.86962.

    Genome annotation databases

    EnsembliENSRNOT00000008980; ENSRNOP00000008980; ENSRNOG00000006364.
    GeneIDi298942.
    KEGGirno:298942.
    UCSCiRGD:735073. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC062069 mRNA. Translation: AAH62069.1 .
    RefSeqi NP_955417.1. NM_199385.2.
    UniGenei Rn.86962.

    3D structure databases

    ProteinModelPortali Q6P6R2.
    SMRi Q6P6R2. Positions 37-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q6P6R2. 1 interaction.
    MINTi MINT-1775384.
    STRINGi 10116.ENSRNOP00000008980.

    PTM databases

    PhosphoSitei Q6P6R2.

    Proteomic databases

    PaxDbi Q6P6R2.
    PRIDEi Q6P6R2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000008980 ; ENSRNOP00000008980 ; ENSRNOG00000006364 .
    GeneIDi 298942.
    KEGGi rno:298942.
    UCSCi RGD:735073. rat.

    Organism-specific databases

    CTDi 1738.
    RGDi 735073. Dld.

    Phylogenomic databases

    eggNOGi COG1249.
    GeneTreei ENSGT00550000074844.
    HOGENOMi HOG000276708.
    HOVERGENi HBG002290.
    KOi K00382.
    OMAi RMERGFV.
    OrthoDBi EOG77126S.
    PhylomeDBi Q6P6R2.
    TreeFami TF300414.

    Enzyme and pathway databases

    Reactomei REACT_203088. Pyruvate metabolism.
    REACT_216424. Citric acid cycle (TCA cycle).
    REACT_220761. Lysine catabolism.
    REACT_221218. Branched-chain amino acid catabolism.
    SABIO-RK Q6P6R2.

    Miscellaneous databases

    NextBioi 644542.
    PROi Q6P6R2.

    Gene expression databases

    Genevestigatori Q6P6R2.

    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. "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].
      Tissue: Prostate.
    2. Lubec G., Afjehi-Sadat L., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 90-104; 289-334; 431-440 AND 483-495, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Spinal cord.

    Entry informationi

    Entry nameiDLDH_RAT
    AccessioniPrimary (citable) accession number: Q6P6R2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3