Overview
| Uniprot ID | P09623 |
|---|
| Protein Name | Dihydrolipoyl dehydrogenase, mitochondrial |
|---|
| Gene Name | DLD |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 143 |
GGIAHLFKQNKVVRV |
| 159 |
GYGKITGKNQVTATK |
| 166 |
KNQVTATKADGSTEV |
| 267 |
NFQRILQKQGFKFKL |
| 277 |
FKFKLNTKVIGATKK |
| 410 |
GKSEEQLKEEGIEYK |
| 417 |
KEEGIEYKVGKFPFA |
| 445 |
MVKILGQKSTDRVLG |
| 66 |
KAAQLGFKTVCIEKN |
Function
Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). The pyruvate dehydrogenase (PDH) complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). The E3 subunit catalyzes reoxidation of the dihydrolipoyl moiety on lipoyl-bearing domains (LBDs) of E2 with NAD+ as the ultimate electron acceptor (By similarity)
Protein Sequence
10
MQSWSRVYCT
20
LAKRGHFNRI
30
AHGLQGVSAV
40
PLRTYADQPI
50
DADVTVIGSG
60
PGGYVAAIKA
70
AQLGFKTVCI
80
EKNETLGGTC
90
LNVGCIPSKA
100
LLNNSHYYHM
110
AHGKDFASRG
120
IEMSEVRLNL
130
EKMMEQKSNA
140
VKALTGGIAH
150
LFKQNKVVRV
160
NGYGKITGKN
170
QVTATKADGS
180
TEVINTKNIL
190
IATGSEVTPF
200
PGITIDEDTV
210
VSSTGALSLK
220
KVPEKMVVIG
230
AGVIGVELGS
240
VWQRLGADVT
250
AVELLGHVGG
260
IGIDMEVSKN
270
FQRILQKQGF
280
KFKLNTKVIG
290
ATKKSDGNID
300
VSIEAASGGK
310
AEVITCDVLL
320
VCIGRRPFTQ
330
NLGLEELGIE
340
LDPRGRIPVN
350
TRFQTKIPNI
360
YAIGDVVAGP
370
MLAHKAEDEG
380
IICVEGMAGG
390
AVHIDYNCVP
400
SVIYTHPEVA
410
WVGKSEEQLK
420
EEGIEYKVGK
430
FPFAANSRAK
440
TNADTDGMVK
450
ILGQKSTDRV
460
LGAHIIGPGA
470
GEMINEAALA
480
LEYGASCEDI
490
ARVCHAHPTL
500
SEAFREANLA
ASFGKAINF
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0001669 |
acrosomal vesicle |
| Cellular Component |
GO:0005759 |
mitochondrial matrix |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Cellular Component |
GO:0031514 |
motile cilium |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0045252 |
oxoglutarate dehydrogenase complex |
| Cellular Component |
GO:0045254 |
pyruvate dehydrogenase complex |
| Molecular Function |
GO:0004148 |
dihydrolipoyl dehydrogenase (NADH) activity |
| Molecular Function |
GO:0050660 |
flavin adenine dinucleotide binding |
| Biological Process |
GO:0006103 |
2-oxoglutarate metabolic process |
| Biological Process |
GO:0006086 |
pyruvate decarboxylation to acetyl-CoA |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.