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Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Fragment)

 DLDH_MESAU              Reviewed;         479 AA.
Q811C4;
15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
22-NOV-2017, entry version 77.
RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial {ECO:0000250|UniProtKB:P09622};
EC=1.8.1.4 {ECO:0000269|PubMed:15888450};
AltName: Full=Dihydrolipoamide dehydrogenase {ECO:0000250|UniProtKB:P09622};
Flags: Precursor; Fragment;
Name=DLD;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1] {ECO:0000305, ECO:0000312|EMBL:CAD61860.1}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-51, FUNCTION, AND
PHOSPHORYLATION.
TISSUE=Sperm {ECO:0000269|PubMed:14645106}, and
Testis {ECO:0000312|EMBL:CAD61860.1};
PubMed=14645106; DOI=10.1095/biolreprod.103.022780;
Mitra K., Shivaji S.;
"Novel tyrosine-phosphorylated post-pyruvate metabolic enzyme,
dihydrolipoamide dehydrogenase, involved in capacitation of hamster
spermatozoa.";
Biol. Reprod. 70:887-899(2004).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND PHOSPHORYLATION.
PubMed=15888450; DOI=10.1074/jbc.M500310200;
Mitra K., Rangaraj N., Shivaji S.;
"Novelty of the pyruvate metabolic enzyme dihydrolipoamide
dehydrogenase in spermatozoa: correlation of its localization,
tyrosine phosphorylation, and activity during sperm capacitation.";
J. Biol. Chem. 280:25743-25753(2005).
[3]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20400973; DOI=10.1038/aja.2010.19;
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B.,
Shivaji S.;
"Glucose-regulated protein precursor (GRP78) and tumor rejection
antigen (GP96) are unique to hamster caput epididymal spermatozoa.";
Asian J. Androl. 12:344-355(2010).
-!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
cleavage system as well as an E3 component of the alpha-ketoacid
dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and
branched-chain amino acid-dehydrogenase complex). In monomeric
form has additional moonlighting function as serine protease (By
similarity). Involved in the hyperactivation of spermatazoa during
capacitation and in the spermatazoal acrosome reaction
(PubMed:14645106, PubMed:15888450). {ECO:0000250|UniProtKB:P09622,
ECO:0000269|PubMed:14645106, ECO:0000269|PubMed:15888450}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH. {ECO:0000269|PubMed:15888450}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:P09622};
Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622};
-!- SUBUNIT: Homodimer. Part of the multimeric pyruvate dehydrogenase
complex that contains multiple copies of pyruvate dehydrogenase
(subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase
(DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits
are bound to an inner core composed of about 48 DLAT and 12 PDHX
molecules (by non covalent bonds). Interacts with PDHX.
{ECO:0000250|UniProtKB:P09622}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:P09622}. Cytoplasmic vesicle, secretory
vesicle, acrosome {ECO:0000269|PubMed:15888450}. Cell projection,
cilium, flagellum {ECO:0000269|PubMed:15888450}.
-!- TISSUE SPECIFICITY: Expressed in testis (at protein level).
{ECO:0000269|PubMed:15888450}.
-!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:14645106,
ECO:0000269|PubMed:15888450}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000250|UniProtKB:P09622}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000255}.
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EMBL; AJ538298; CAD61860.1; -; mRNA.
ProteinModelPortal; Q811C4; -.
PRIDE; Q811C4; -.
HOVERGEN; HBG002290; -.
BRENDA; 1.8.1.4; 3239.
Proteomes; UP000189706; Genome assembly.
GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
Gene3D; 3.30.390.30; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
Acetylation; Cell projection; Cilium; Complete proteome;
Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; FAD;
Flagellum; Flavoprotein; Mitochondrion; NAD; Oxidoreductase;
Phosphoprotein; Redox-active center; Reference proteome;
Transit peptide.
TRANSIT <1 19 Mitochondrion.
{ECO:0000269|PubMed:14645106}.
CHAIN 20 >479 Dihydrolipoyl dehydrogenase,
mitochondrial.
{ECO:0000269|PubMed:14645106}.
/FTId=PRO_5000070424.
NP_BIND 55 64 FAD. {ECO:0000250|UniProtKB:P09622}.
NP_BIND 167 169 FAD. {ECO:0000250|UniProtKB:P09622}.
NP_BIND 204 211 NAD. {ECO:0000250|UniProtKB:P09622}.
NP_BIND 345 348 FAD. {ECO:0000250|UniProtKB:P09622}.
ACT_SITE 471 471 Proton acceptor.
{ECO:0000250|UniProtKB:P09624}.
BINDING 73 73 FAD. {ECO:0000250|UniProtKB:P09622}.
BINDING 138 138 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:P09622}.
BINDING 227 227 NAD. {ECO:0000250|UniProtKB:P09622}.
BINDING 262 262 NAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:P09622}.
BINDING 298 298 NAD; via amide nitrogen.
{ECO:0000250|UniProtKB:P09622}.
BINDING 339 339 FAD. {ECO:0000250|UniProtKB:P09622}.
SITE 432 432 Important for interaction with PDHX and
activity of pyruvate dehydrogenase
complex. {ECO:0000250|UniProtKB:P09622}.
SITE 457 457 Important for interaction with PDHX and
activity of pyruvate dehydrogenase
complex. {ECO:0000250|UniProtKB:P09622}.
MOD_RES 50 50 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 50 50 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 88 88 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 88 88 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 106 106 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 106 106 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 116 116 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 116 116 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 127 127 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P09622}.
MOD_RES 127 127 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 143 143 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 150 150 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 257 257 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 261 261 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 330 330 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 394 394 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P09622}.
MOD_RES 394 394 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 401 401 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09622}.
MOD_RES 404 404 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 414 414 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
DISULFID 64 69 Redox-active.
{ECO:0000250|UniProtKB:P09622}.
NON_TER 1 1 {ECO:0000312|EMBL:CAD61860.1}.
NON_TER 479 479 {ECO:0000312|EMBL:CAD61860.1}.
SEQUENCE 479 AA; 50723 MW; 1F2EA60777B3DCE4 CRC64;
FNRXSPGLQG VSSVPLRTYA DQPIDADVTV IGSGPGGYVA AIKAAQLGFK TVCIEKNETL
GGTCLNVGCI PSKALLNNSH YYHLAHGKDF ASRGIELSEV RLNLEKMMEQ KSSAVKALTG
GIAHLFKQNK VVHVNGFGNI TGKNQVTATK ADGSSQVIGT KNILIATGSE VTPFPGITID
EDTIVSSTGA LSLKKVPEKL VVIGAGVIGV ELGSVWQRLG AEVTAVEFLG HVGGIGIDME
ISKKFQRILQ KQGFKFKLNP KVPGATKRSD GKIDVSVEAA PGGKAEVIPC DVLLVCIGRR
PFTQNLGLEE LGIELDPRGR IPVNTRFQTK IPNIYAIGDV VAGPMLAHKA EDEGIICVEG
MAGGAVHIDY NCVPSVIYTH PEVAWVGKSE EQLKEEGIEY KVGKFPFAAN SRAKTNADTD
GMVKILGQKS TDRVLGAHIL GPGAGEMVNE AALALEYGAS CEDIARVCHA HPTLSEAFR


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