CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015197
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydrolipoyl dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 Dihydrolipoamide dehydrogenase 
Gene Name
 Dld 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
104YYHLAHGKDFASRGIacetylation[1]
132EQKRSAVKALTGGIAacetylation[1]
143GGIAHLFKQNKVVHVacetylation[1]
159GFGKITGKNQVTATTacetylation[1]
267NFQRILQKQGFKFKLacetylation[1]
273QKQGFKFKLNTKVTGacetylation[1]
277FKFKLNTKVTGATKKacetylation[1]
334LGIELDPKGRIPVNTacetylation[1]
346VNTRFQTKIPNIFAIacetylation[1]
440ADTDGMVKILGHKSTacetylation[1]
445MVKILGHKSTDRILGacetylation[1]
505NLAASFGKPINF***acetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 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). 
Sequence Annotation
 NP_BIND 71 80 FAD (By similarity).
 NP_BIND 183 185 FAD (By similarity).
 NP_BIND 220 227 NAD (By similarity).
 NP_BIND 361 364 FAD (By similarity).
 ACT_SITE 487 487 Proton acceptor (By similarity).
 BINDING 89 89 FAD (By similarity).
 BINDING 154 154 FAD; via amide nitrogen and carbonyl
 BINDING 243 243 NAD (By similarity).
 BINDING 278 278 NAD; via amide nitrogen and carbonyl
 BINDING 314 314 NAD; via amide nitrogen (By similarity).
 BINDING 355 355 FAD (By similarity).
 MOD_RES 127 127 N6-acetyllysine (By similarity).
 MOD_RES 143 143 N6-acetyllysine (By similarity).
 MOD_RES 410 410 N6-acetyllysine (By similarity).
 MOD_RES 417 417 N6-acetyllysine (By similarity).
 DISULFID 80 85 Redox-active (By similarity).  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein; Redox-active center; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 509 AA 
Protein Sequence
MQSWSRVYCS LAKKGHFNRL SHGLQGASSV PLRTYSDQPI DADVTVIGSG PGGYVAAIKA 60
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHL AHGKDFASRG IEIPEVRLNL 120
EKMMEQKRSA VKALTGGIAH LFKQNKVVHV NGFGKITGKN QVTATTADGS TQVIGTKNIL 180
IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT 240
AVEFLGHVGG IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK 300
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN TRFQTKIPNI FAIGDVVAGP 360
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGVEFKVGK 420
FPFAANSRAK TNADTDGMVK ILGHKSTDRI LGAHILGPGA GEMVNEAALA LEYGASCEDV 480
ARVCHAHPTL SEAFREANLA ASFGKPINF 509 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:RGD.
 GO:0045252; C:oxoglutarate dehydrogenase complex; IDA:RGD.
 GO:0045254; C:pyruvate dehydrogenase complex; IDA:RGD.
 GO:0004148; F:dihydrolipoyl dehydrogenase activity; IDA:RGD.
 GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
 GO:0043544; F:lipoamide binding; IDA:RGD.
 GO:0051287; F:NAD binding; IDA:RGD.
 GO:0006103; P:2-oxoglutarate metabolic process; IDA:RGD.
 GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:RGD.
 GO:0007568; P:aging; IEP:RGD.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0051068; P:dihydrolipoamide metabolic process; IDA:RGD.
 GO:0009106; P:lipoate metabolic process; IDA:RGD. 
Interpro
 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. 
Pfam
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2
 PF02852; Pyr_redox_dim 
SMART
  
PROSITE
 PS00076; PYRIDINE_REDOX_1 
PRINTS
 PR00368; FADPNR.