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)

P09622

- DLDH_HUMAN

UniProt

P09622 - DLDH_HUMAN

Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

DLD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 185 (01 Oct 2014)
      Sequence version 2 (24 Nov 2009)
      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 – 891FAD
    Binding sitei154 – 1541FAD; via amide nitrogen and carbonyl oxygen
    Binding sitei243 – 2431NAD
    Binding sitei278 – 2781NAD; via amide nitrogen and carbonyl oxygen
    Binding sitei314 – 3141NAD; via amide nitrogen
    Binding sitei355 – 3551FAD
    Active sitei487 – 4871Proton acceptorBy similarity

    Regions

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

    GO - Molecular functioni

    1. dihydrolipoyl dehydrogenase activity Source: ProtInc
    2. flavin adenine dinucleotide binding Source: InterPro
    3. oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor Source: InterPro

    GO - Biological processi

    1. branched-chain amino acid catabolic process Source: Reactome
    2. cell redox homeostasis Source: InterPro
    3. cellular metabolic process Source: Reactome
    4. cellular nitrogen compound metabolic process Source: Reactome
    5. gastrulation Source: Ensembl
    6. lysine catabolic process Source: Reactome
    7. mitochondrial electron transport, NADH to ubiquinone Source: Ensembl
    8. proteolysis Source: Ensembl
    9. pyruvate metabolic process Source: Reactome
    10. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
    11. regulation of membrane potential Source: Ensembl
    12. small molecule metabolic process Source: Reactome
    13. sperm capacitation Source: Ensembl
    14. tricarboxylic acid cycle Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01727-MONOMER.
    ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_1298. Lysine catabolism.
    REACT_1785. Citric acid cycle (TCA cycle).
    REACT_197. Branched-chain amino acid catabolism.
    REACT_2071. Pyruvate metabolism.
    SABIO-RKP09622.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4)
    Alternative name(s):
    Dihydrolipoamide dehydrogenase
    Glycine cleavage system L protein
    Gene namesi
    Name:DLD
    Synonyms:GCSL, LAD, PHE3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:2898. DLD.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal matrix Source: Ensembl
    2. cilium Source: Ensembl
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: UniProt
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Dihydrolipoamide dehydrogenase deficiency (DLDD) [MIM:246900]: An autosomal recessive metabolic disorder characterized biochemically by a combined deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate dehydrogenase complex (KGDC). Clinically, affected individuals have lactic acidosis and neurologic deterioration due to sensitivity of the central nervous system to defects in oxidative metabolism.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721K → E in DLDD. 1 Publication
    VAR_006907
    Natural varianti229 – 2291G → C in DLDD. 1 Publication
    VAR_015820
    Natural varianti488 – 4881P → L in DLDD. 1 Publication
    VAR_006908
    Natural varianti495 – 4951R → G in DLDD; loss of enzyme activity. 1 Publication
    VAR_015821

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi246900. phenotype.
    Orphaneti255249. Leigh syndrome with nephrotic syndrome.
    2394. Pyruvate dehydrogenase E3 deficiency.
    PharmGKBiPA27352.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535MitochondrionAdd
    BLAST
    Chaini36 – 509474Dihydrolipoyl dehydrogenase, mitochondrialPRO_0000030295Add
    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-active
    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; alternate1 Publication
    Modified residuei143 – 1431N6-succinyllysine; alternateBy similarity
    Modified residuei159 – 1591N6-succinyllysineBy similarity
    Modified residuei166 – 1661N6-succinyllysineBy similarity
    Modified residuei273 – 2731N6-succinyllysineBy similarity
    Modified residuei277 – 2771N6-succinyllysineBy similarity
    Modified residuei346 – 3461N6-acetyllysineBy similarity
    Modified residuei410 – 4101N6-acetyllysine; alternate1 Publication
    Modified residuei410 – 4101N6-succinyllysine; alternateBy similarity
    Modified residuei417 – 4171N6-acetyllysine1 Publication
    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

    MaxQBiP09622.
    PaxDbiP09622.
    PRIDEiP09622.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00015911.
    UCD-2DPAGEP09622.

    PTM databases

    PhosphoSiteiP09622.

    Expressioni

    Gene expression databases

    ArrayExpressiP09622.
    BgeeiP09622.
    CleanExiHS_DLD.
    GenevestigatoriP09622.

    Organism-specific databases

    HPAiHPA044849.

    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.2 Publications

    Protein-protein interaction databases

    BioGridi108082. 36 interactions.
    DIPiDIP-29027N.
    IntActiP09622. 7 interactions.
    MINTiMINT-3007138.
    STRINGi9606.ENSP00000205402.

    Structurei

    Secondary structure

    1
    509
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 478
    Helixi51 – 6212
    Beta strandi67 – 715
    Beta strandi73 – 775
    Helixi78 – 836
    Helixi85 – 10218
    Helixi105 – 1084
    Beta strandi111 – 1144
    Beta strandi116 – 1183
    Helixi120 – 14425
    Beta strandi148 – 15811
    Beta strandi161 – 1655
    Beta strandi171 – 18111
    Beta strandi185 – 1873
    Beta strandi197 – 2015
    Helixi203 – 2064
    Beta strandi214 – 2196
    Helixi223 – 23412
    Beta strandi238 – 2425
    Beta strandi244 – 2496
    Helixi255 – 26713
    Beta strandi271 – 2733
    Beta strandi275 – 2839
    Beta strandi289 – 2957
    Beta strandi302 – 31110
    Beta strandi315 – 3173
    Helixi324 – 3274
    Beta strandi350 – 3523
    Helixi354 – 3563
    Beta strandi357 – 3593
    Helixi363 – 37715
    Helixi386 – 3883
    Beta strandi391 – 3933
    Beta strandi395 – 4039
    Helixi406 – 4127
    Beta strandi416 – 4227
    Helixi423 – 4253
    Helixi427 – 4315
    Beta strandi438 – 4447
    Turni445 – 4473
    Beta strandi449 – 4579
    Helixi460 – 47314
    Helixi477 – 4826
    Helixi491 – 50313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZMCX-ray2.53A/B/C/D/E/F/G/H36-509[»]
    1ZMDX-ray2.08A/B/C/D/E/F/G/H36-509[»]
    1ZY8X-ray2.59A/B/C/D/E/F/G/H/I/J36-509[»]
    2F5ZX-ray2.18A/B/C/D/E/F/G/H/I/J36-509[»]
    3RNMX-ray2.40A/B/C/D36-509[»]
    ProteinModelPortaliP09622.
    SMRiP09622. Positions 37-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09622.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276708.
    HOVERGENiHBG002290.
    InParanoidiP09622.
    KOiK00382.
    OMAiENLNLDM.
    OrthoDBiEOG77126S.
    PhylomeDBiP09622.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P09622-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQSWSRVYCS LAKRGHFNRI SHGLQGLSAV PLRTYADQPI DADVTVIGSG    50
    PGGYVAAIKA AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM 100
    AHGKDFASRG IEMSEVRLNL DKMMEQKSTA VKALTGGIAH LFKQNKVVHV 150
    NGYGKITGKN QVTATKADGG TQVIDTKNIL IATGSEVTPF PGITIDEDTI 200
    VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG 250
    VGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK 300
    AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQTKIPNI 350
    YAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA 400
    WVGKSEEQLK EEGIEYKVGK FPFAANSRAK TNADTDGMVK ILGQKSTDRV 450
    LGAHILGPGA GEMVNEAALA LEYGASCEDI ARVCHAHPTL SEAFREANLA 500
    ASFGKSINF 509
    Length:509
    Mass (Da):54,177
    Last modified:November 24, 2009 - v2
    Checksum:i7613492C516F3835
    GO
    Isoform 2 (identifier: P09622-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-99: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:410
    Mass (Da):43,587
    Checksum:i4FB4B37B7A801353
    GO
    Isoform 3 (identifier: P09622-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         147-194: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:461
    Mass (Da):49,283
    Checksum:iE9BB766499627F76
    GO

    Sequence cautioni

    The sequence BAD92940.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti154 – 1541G → R in AAA35764. (PubMed:3278312)Curated
    Sequence conflicti209 – 2091L → F in BAD92940. 1 PublicationCurated
    Sequence conflicti493 – 4931A → AEA in AAB01381. (PubMed:8406489)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721K → E in DLDD. 1 Publication
    VAR_006907
    Natural varianti104 – 1041K → T.2 Publications
    Corresponds to variant rs1130477 [ dbSNP | Ensembl ].
    VAR_031922
    Natural varianti229 – 2291G → C in DLDD. 1 Publication
    VAR_015820
    Natural varianti331 – 3311L → V.
    Corresponds to variant rs17624 [ dbSNP | Ensembl ].
    VAR_014555
    Natural varianti488 – 4881P → L in DLDD. 1 Publication
    VAR_006908
    Natural varianti495 – 4951R → G in DLDD; loss of enzyme activity. 1 Publication
    VAR_015821

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9999Missing in isoform 2. 1 PublicationVSP_055855Add
    BLAST
    Alternative sequencei147 – 19448Missing in isoform 3. 1 PublicationVSP_055856Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03490 mRNA. Translation: AAA59527.1.
    J03620 mRNA. Translation: AAA35764.1.
    L13761
    , L13749, L13750, L13751, L13752, L13753, L13754, L13748, L13755, L13759, L13760, L13756, L13757, L13758 Genomic DNA. Translation: AAB01381.1.
    AK295080 mRNA. Translation: BAG58122.1.
    AK300077 mRNA. Translation: BAG61881.1.
    AK312346 mRNA. Translation: BAG35267.1.
    AB209703 mRNA. Translation: BAD92940.1. Different initiation.
    AC005046 Genomic DNA. No translation available.
    CH236947 Genomic DNA. Translation: EAL24389.1.
    CH471070 Genomic DNA. Translation: EAW83421.1.
    BC018648 mRNA. Translation: AAH18648.1.
    BC018696 mRNA. Translation: AAH18696.1.
    M99384 Genomic DNA. Translation: AAA35759.1.
    CCDSiCCDS5749.1.
    PIRiA92622. DEHULP.
    RefSeqiNP_000099.2. NM_000108.4.
    NP_001276680.1. NM_001289751.1.
    NP_001276681.1. NM_001289752.1.
    UniGeneiHs.131711.

    Genome annotation databases

    EnsembliENST00000205402; ENSP00000205402; ENSG00000091140. [P09622-1]
    ENST00000417551; ENSP00000390667; ENSG00000091140. [P09622-1]
    ENST00000437604; ENSP00000387542; ENSG00000091140. [P09622-3]
    GeneIDi1738.
    KEGGihsa:1738.
    UCSCiuc003vet.3. human.

    Polymorphism databases

    DMDMi269849557.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03490 mRNA. Translation: AAA59527.1 .
    J03620 mRNA. Translation: AAA35764.1 .
    L13761
    , L13749 , L13750 , L13751 , L13752 , L13753 , L13754 , L13748 , L13755 , L13759 , L13760 , L13756 , L13757 , L13758 Genomic DNA. Translation: AAB01381.1 .
    AK295080 mRNA. Translation: BAG58122.1 .
    AK300077 mRNA. Translation: BAG61881.1 .
    AK312346 mRNA. Translation: BAG35267.1 .
    AB209703 mRNA. Translation: BAD92940.1 . Different initiation.
    AC005046 Genomic DNA. No translation available.
    CH236947 Genomic DNA. Translation: EAL24389.1 .
    CH471070 Genomic DNA. Translation: EAW83421.1 .
    BC018648 mRNA. Translation: AAH18648.1 .
    BC018696 mRNA. Translation: AAH18696.1 .
    M99384 Genomic DNA. Translation: AAA35759.1 .
    CCDSi CCDS5749.1.
    PIRi A92622. DEHULP.
    RefSeqi NP_000099.2. NM_000108.4.
    NP_001276680.1. NM_001289751.1.
    NP_001276681.1. NM_001289752.1.
    UniGenei Hs.131711.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZMC X-ray 2.53 A/B/C/D/E/F/G/H 36-509 [» ]
    1ZMD X-ray 2.08 A/B/C/D/E/F/G/H 36-509 [» ]
    1ZY8 X-ray 2.59 A/B/C/D/E/F/G/H/I/J 36-509 [» ]
    2F5Z X-ray 2.18 A/B/C/D/E/F/G/H/I/J 36-509 [» ]
    3RNM X-ray 2.40 A/B/C/D 36-509 [» ]
    ProteinModelPortali P09622.
    SMRi P09622. Positions 37-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108082. 36 interactions.
    DIPi DIP-29027N.
    IntActi P09622. 7 interactions.
    MINTi MINT-3007138.
    STRINGi 9606.ENSP00000205402.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P09622.

    Polymorphism databases

    DMDMi 269849557.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00015911.
    UCD-2DPAGE P09622.

    Proteomic databases

    MaxQBi P09622.
    PaxDbi P09622.
    PRIDEi P09622.

    Protocols and materials databases

    DNASUi 1738.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000205402 ; ENSP00000205402 ; ENSG00000091140 . [P09622-1 ]
    ENST00000417551 ; ENSP00000390667 ; ENSG00000091140 . [P09622-1 ]
    ENST00000437604 ; ENSP00000387542 ; ENSG00000091140 . [P09622-3 ]
    GeneIDi 1738.
    KEGGi hsa:1738.
    UCSCi uc003vet.3. human.

    Organism-specific databases

    CTDi 1738.
    GeneCardsi GC07P107531.
    H-InvDB HIX0006994.
    HGNCi HGNC:2898. DLD.
    HPAi HPA044849.
    MIMi 238331. gene.
    246900. phenotype.
    neXtProti NX_P09622.
    Orphaneti 255249. Leigh syndrome with nephrotic syndrome.
    2394. Pyruvate dehydrogenase E3 deficiency.
    PharmGKBi PA27352.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276708.
    HOVERGENi HBG002290.
    InParanoidi P09622.
    KOi K00382.
    OMAi ENLNLDM.
    OrthoDBi EOG77126S.
    PhylomeDBi P09622.
    TreeFami TF300414.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01727-MONOMER.
    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_1298. Lysine catabolism.
    REACT_1785. Citric acid cycle (TCA cycle).
    REACT_197. Branched-chain amino acid catabolism.
    REACT_2071. Pyruvate metabolism.
    SABIO-RK P09622.

    Miscellaneous databases

    EvolutionaryTracei P09622.
    GeneWikii Dihydrolipoamide_dehydrogenase.
    GenomeRNAii 1738.
    NextBioi 7047.
    PROi P09622.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09622.
    Bgeei P09622.
    CleanExi HS_DLD.
    Genevestigatori P09622.

    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. "Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases."
      Otulakowski G., Robinson B.H.
      J. Biol. Chem. 262:17313-17318(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-104.
    2. "Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes."
      Pons G., Raefsky-Estrin C., Carothers D.J., Pepin R.A., Javed A.A., Jesse B.W., Ganapathi M.K., Samols D., Patel M.S.
      Proc. Natl. Acad. Sci. U.S.A. 85:1422-1426(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements."
      Feigenbaum A.S., Robinson B.H.
      Genomics 17:376-381(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-104.
      Tissue: Liver.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Brain, Brain cortex and Pericardium.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1).
      Tissue: Ovary.
    10. "Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene."
      Johanning G.L., Morris J.I., Madhusudhan K.T., Samols D., Patel M.S.
      Proc. Natl. Acad. Sci. U.S.A. 89:10964-10968(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143; LYS-410 AND LYS-417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations."
      Brautigam C.A., Chuang J.L., Tomchick D.R., Machius M., Chuang D.T.
      J. Mol. Biol. 350:543-552(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 36-509 IN COMPLEXES WITH NAD AND FAD, SUBUNIT.
    14. "How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex."
      Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K., Korotchkina L.G., Patel M.S.
      J. Biol. Chem. 281:648-655(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 36-509.
    15. "Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex."
      Brautigam C.A., Wynn R.M., Chuang J.L., Machius M., Tomchick D.R., Chuang D.T.
      Structure 14:611-621(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 36-509 IN COMPLEX WITH PDHX, CHARACTERIZATION OF VARIANT DLDD GLY-495.
    16. "Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient."
      Liu T.-C., Kim H., Arizmendi C., Kitano A., Patel M.S.
      Proc. Natl. Acad. Sci. U.S.A. 90:5186-5190(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DLDD GLU-72 AND LEU-488.
    17. "Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency."
      Hong Y.S., Kerr D.S., Craigen W.J., Tan J., Pan Y., Lusk M., Patel M.S.
      Hum. Mol. Genet. 5:1925-1930(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DLDD GLY-495.
    18. "Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews."
      Shaag A., Saada A., Berger I., Mandel H., Joseph A., Feigenbaum A., Elpeleg O.N.
      Am. J. Med. Genet. 82:177-182(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DLDD CYS-229.

    Entry informationi

    Entry nameiDLDH_HUMAN
    AccessioniPrimary (citable) accession number: P09622
    Secondary accession number(s): B2R5X0
    , B4DHG0, B4DT69, Q14131, Q14167, Q59EV8, Q8WTS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 185 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3