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P09622 (DLDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase, mitochondrial

EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
Glycine cleavage system L protein
Gene names
Name:DLD
Synonyms:GCSL, LAD, PHE3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

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. Ref.12

Subcellular location

Mitochondrion matrix.

Post-translational modification

Tyrosine phosphorylated By similarity.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16 Ref.17

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRedox-active center
Transit peptide
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbranched-chain amino acid catabolic process

Traceable author statement. Source: Reactome

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular metabolic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gastrulation

Inferred from electronic annotation. Source: Ensembl

lysine catabolic process

Traceable author statement. Source: Reactome

mitochondrial electron transport, NADH to ubiquinone

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from electronic annotation. Source: Ensembl

pyruvate metabolic process

Traceable author statement. Source: Reactome

regulation of acetyl-CoA biosynthetic process from pyruvate

Traceable author statement. Source: Reactome

regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sperm capacitation

Inferred from electronic annotation. Source: Ensembl

tricarboxylic acid cycle

Traceable author statement. Source: Reactome

   Cellular_componentacrosomal matrix

Inferred from electronic annotation. Source: Ensembl

cilium

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functiondihydrolipoyl dehydrogenase activity

Traceable author statement Ref.15. Source: ProtInc

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion
Chain36 – 509474Dihydrolipoyl dehydrogenase, mitochondrial
PRO_0000030295

Regions

Nucleotide binding71 – 8010FAD
Nucleotide binding183 – 1853FAD
Nucleotide binding220 – 2278NAD
Nucleotide binding361 – 3644FAD

Sites

Active site4871Proton acceptor By similarity
Binding site891FAD
Binding site1541FAD; via amide nitrogen and carbonyl oxygen
Binding site2431NAD
Binding site2781NAD; via amide nitrogen and carbonyl oxygen
Binding site3141NAD; via amide nitrogen
Binding site3551FAD

Amino acid modifications

Modified residue661N6-acetyllysine; alternate By similarity
Modified residue661N6-succinyllysine; alternate By similarity
Modified residue1041N6-acetyllysine; alternate By similarity
Modified residue1041N6-succinyllysine; alternate By similarity
Modified residue1221N6-acetyllysine; alternate By similarity
Modified residue1221N6-succinyllysine; alternate By similarity
Modified residue1321N6-acetyllysine; alternate By similarity
Modified residue1321N6-succinyllysine; alternate By similarity
Modified residue1431N6-acetyllysine; alternate Ref.10
Modified residue1431N6-succinyllysine; alternate By similarity
Modified residue1591N6-succinyllysine By similarity
Modified residue1661N6-succinyllysine By similarity
Modified residue2731N6-succinyllysine By similarity
Modified residue2771N6-succinyllysine By similarity
Modified residue3461N6-acetyllysine By similarity
Modified residue4101N6-acetyllysine; alternate Ref.10
Modified residue4101N6-succinyllysine; alternate By similarity
Modified residue4171N6-acetyllysine Ref.10
Modified residue4201N6-acetyllysine By similarity
Modified residue4301N6-succinyllysine By similarity
Modified residue5051N6-acetyllysine; alternate By similarity
Modified residue5051N6-succinyllysine; alternate By similarity
Disulfide bond80 ↔ 85Redox-active

Natural variations

Natural variant721K → E in DLDD. Ref.15
VAR_006907
Natural variant1041K → T. Ref.1 Ref.3
Corresponds to variant rs1130477 [ dbSNP | Ensembl ].
VAR_031922
Natural variant2291G → C in DLDD. Ref.17
VAR_015820
Natural variant3311L → V.
Corresponds to variant rs17624 [ dbSNP | Ensembl ].
VAR_014555
Natural variant4881P → L in DLDD. Ref.15
VAR_006908
Natural variant4951R → G in DLDD; loss of enzyme activity. Ref.14 Ref.16
VAR_015821

Experimental info

Sequence conflict1541G → R in AAA35764. Ref.2
Sequence conflict2091L → F in BAD92940. Ref.5
Sequence conflict4931A → AEA in AAB01381. Ref.3

Secondary structure

..................................................................................... 509
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09622 [UniParc].

Last modified November 24, 2009. Version 2.
Checksum: 7613492C516F3835

FASTA50954,177
        10         20         30         40         50         60 
MQSWSRVYCS LAKRGHFNRI SHGLQGLSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA 

        70         80         90        100        110        120 
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL 

       130        140        150        160        170        180 
DKMMEQKSTA VKALTGGIAH LFKQNKVVHV NGYGKITGKN QVTATKADGG TQVIDTKNIL 

       190        200        210        220        230        240 
IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT 

       250        260        270        280        290        300 
AVEFLGHVGG VGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK 

       310        320        330        340        350        360 
AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP 

       370        380        390        400        410        420 
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK 

       430        440        450        460        470        480 
FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI 

       490        500 
ARVCHAHPTL SEAFREANLA ASFGKSINF 

« Hide

References

« Hide 'large scale' references
[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], 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].
[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. expand/collapse author list , 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].
Tissue: Brain cortex.
[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].
Tissue: Brain.
[6]"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. expand/collapse author list , 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].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Ovary.
[9]"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.
[10]"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].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03490 mRNA. Translation: AAA59527.1.
J03620 mRNA. Translation: AAA35764.1.
L13761 expand/collapse EMBL AC list , L13749, L13750, L13751, L13752, L13753, L13754, L13748, L13755, L13759, L13760, L13756, L13757, L13758 Genomic DNA. Translation: AAB01381.1.
AK312346 mRNA. Translation: BAG35267.1.
AB209703 mRNA. Translation: BAD92940.1. Different initiation.
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.
PIRDEHULP. A92622.
RefSeqNP_000099.2. NM_000108.4.
UniGeneHs.131711.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP09622.
SMRP09622. Positions 37-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108082. 33 interactions.
DIPDIP-29027N.
IntActP09622. 7 interactions.
MINTMINT-3007138.
STRING9606.ENSP00000205402.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP09622.

Polymorphism databases

DMDM269849557.

2D gel databases

REPRODUCTION-2DPAGEIPI00015911.
UCD-2DPAGEP09622.

Proteomic databases

PaxDbP09622.
PRIDEP09622.

Protocols and materials databases

DNASU1738.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000205402; ENSP00000205402; ENSG00000091140.
ENST00000417551; ENSP00000390667; ENSG00000091140.
GeneID1738.
KEGGhsa:1738.
UCSCuc003vet.3. human.

Organism-specific databases

CTD1738.
GeneCardsGC07P107531.
H-InvDBHIX0006994.
HGNCHGNC:2898. DLD.
HPAHPA044849.
MIM238331. gene.
246900. phenotype.
neXtProtNX_P09622.
Orphanet268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
255249. Leigh syndrome with nephrotic syndrome.
2394. Pyruvate dehydrogenase E3 deficiency.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBPA27352.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276708.
HOVERGENHBG002290.
InParanoidP09622.
KOK00382.
OMAIDSEYRT.
OrthoDBEOG77126S.
PhylomeDBP09622.
TreeFamTF300414.

Enzyme and pathway databases

BioCycMetaCyc:HS01727-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP09622.

Gene expression databases

ArrayExpressP09622.
BgeeP09622.
CleanExHS_DLD.
GenevestigatorP09622.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. 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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09622.
GeneWikiDihydrolipoamide_dehydrogenase.
GenomeRNAi1738.
NextBio7047.
PROP09622.
SOURCESearch...

Entry information

Entry nameDLDH_HUMAN
AccessionPrimary (citable) accession number: P09622
Secondary accession number(s): B2R5X0 expand/collapse secondary AC list , Q14131, Q14167, Q59EV8, Q8WTS4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 24, 2009
Last modified: April 16, 2014
This is version 180 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM