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Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein) (Pyruvate dehydrogenase complex E3 subunit) (E3) (PDC-E3)

 DLDH_PEA                Reviewed;         501 AA.
P31023;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
11-JUL-2001, sequence version 2.
22-NOV-2017, entry version 126.
RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=Glycine cleavage system L protein;
AltName: Full=Pyruvate dehydrogenase complex E3 subunit;
Short=E3;
Short=PDC-E3;
Flags: Precursor;
Name=LPD;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leaf;
PubMed=1541297; DOI=10.1111/j.1432-1033.1992.tb16706.x;
Bourguignon J., Macherel D., Neuburger M., Douce R.;
"Isolation, characterization, and sequence analysis of a cDNA clone
encoding L-protein, the dihydrolipoamide dehydrogenase component of
the glycine cleavage system from pea-leaf mitochondria.";
Eur. J. Biochem. 204:865-873(1992).
[2]
SEQUENCE REVISION TO 480.
Bourguignon J.;
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Birte; TISSUE=Leaf;
PubMed=1560008;
Turner S.R., Ireland R., Rawsthorne S.;
"Purification and primary amino acid sequence of the L subunit of
glycine decarboxylase. Evidence for a single lipoamide dehydrogenase
in plant mitochondria.";
J. Biol. Chem. 267:7745-7750(1992).
[4]
SEQUENCE REVISION TO 499-501.
Rawsthorne S.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 32-61 AND 493-501, AND MASS SPECTROMETRY.
PubMed=8546688; DOI=10.1042/bj3130229;
Bourguignon J., Merand V., Rawsthorne S., Forest E., Douce R.;
"Glycine decarboxylase and pyruvate dehydrogenase complexes share the
same dihydrolipoamide dehydrogenase in pea leaf mitochondria: evidence
from mass spectrometry and primary-structure analysis.";
Biochem. J. 313:229-234(1996).
[6]
X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 32-501 IN COMPLEX WITH FAD,
SUBUNIT, AND DISULFIDE BOND.
PubMed=10806386; DOI=10.1046/j.1432-1033.2000.01330.x;
Faure M., Bourguignon J., Neuburger M., MacHerel D., Sieker L.,
Ober R., Kahn R., Cohen-Addad C., Douce R.;
"Interaction between the lipoamide-containing H-protein and the
lipoamide dehydrogenase (L-protein) of the glycine decarboxylase
multienzyme system 2. Crystal structures of H- and L-proteins.";
Eur. J. Biochem. 267:2890-2898(2000).
[7]
ERRATUM.
Faure M., Bourguignon J., Neuburger M., MacHerel D., Sieker L.,
Ober R., Kahn R., Cohen-Addad C., Douce R.;
Eur. J. Biochem. 267:3914-3914(2000).
-!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
cleavage system as well as of the alpha-ketoacid dehydrogenase
complexes. The pyruvate dehydrogenase complex contains multiple
copies of three enzymatic components: pyruvate dehydrogenase (E1),
dihydrolipoamide acetyltransferase (E2) and lipoamide
dehydrogenase (E3).
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10806386}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- MASS SPECTROMETRY: Mass=49753; Mass_error=5; Method=Electrospray;
Range=32-501; Evidence={ECO:0000269|PubMed:8546688};
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X63464; CAA45066.2; -; mRNA.
EMBL; X62995; CAA44729.1; -; mRNA.
PIR; S22384; S22384.
PDB; 1DXL; X-ray; 3.15 A; A/B/C/D=32-501.
PDBsum; 1DXL; -.
ProteinModelPortal; P31023; -.
SMR; P31023; -.
IntAct; P31023; 1.
PRIDE; P31023; -.
SABIO-RK; P31023; -.
EvolutionaryTrace; P31023; -.
GO; GO:0005960; C:glycine cleavage complex; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:CACAO.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IDA:CACAO.
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.
Gene3D; 3.50.50.60; -; 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;
3D-structure; Direct protein sequencing; Disulfide bond; FAD;
Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Redox-active center;
Transit peptide.
TRANSIT 1 31 Mitochondrion.
{ECO:0000269|PubMed:8546688}.
CHAIN 32 501 Dihydrolipoyl dehydrogenase,
mitochondrial.
/FTId=PRO_0000030299.
NP_BIND 67 76 FAD. {ECO:0000269|PubMed:10806386}.
NP_BIND 178 180 FAD. {ECO:0000250}.
NP_BIND 215 222 NAD. {ECO:0000250}.
NP_BIND 354 357 FAD. {ECO:0000269|PubMed:10806386}.
ACT_SITE 480 480 Proton acceptor. {ECO:0000250}.
BINDING 85 85 FAD. {ECO:0000250}.
BINDING 149 149 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:10806386}.
BINDING 238 238 NAD. {ECO:0000250}.
BINDING 272 272 NAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 307 307 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 348 348 FAD. {ECO:0000269|PubMed:10806386}.
DISULFID 76 81 Redox-active.
{ECO:0000269|PubMed:10806386}.
STRAND 40 43 {ECO:0000244|PDB:1DXL}.
HELIX 47 58 {ECO:0000244|PDB:1DXL}.
STRAND 63 67 {ECO:0000244|PDB:1DXL}.
STRAND 69 72 {ECO:0000244|PDB:1DXL}.
HELIX 76 79 {ECO:0000244|PDB:1DXL}.
HELIX 81 99 {ECO:0000244|PDB:1DXL}.
HELIX 102 104 {ECO:0000244|PDB:1DXL}.
STRAND 106 109 {ECO:0000244|PDB:1DXL}.
STRAND 111 113 {ECO:0000244|PDB:1DXL}.
HELIX 115 140 {ECO:0000244|PDB:1DXL}.
STRAND 143 147 {ECO:0000244|PDB:1DXL}.
STRAND 149 153 {ECO:0000244|PDB:1DXL}.
STRAND 156 159 {ECO:0000244|PDB:1DXL}.
STRAND 162 164 {ECO:0000244|PDB:1DXL}.
STRAND 167 170 {ECO:0000244|PDB:1DXL}.
STRAND 172 176 {ECO:0000244|PDB:1DXL}.
STRAND 180 182 {ECO:0000244|PDB:1DXL}.
STRAND 192 196 {ECO:0000244|PDB:1DXL}.
HELIX 198 201 {ECO:0000244|PDB:1DXL}.
STRAND 209 214 {ECO:0000244|PDB:1DXL}.
HELIX 218 230 {ECO:0000244|PDB:1DXL}.
STRAND 233 237 {ECO:0000244|PDB:1DXL}.
STRAND 239 244 {ECO:0000244|PDB:1DXL}.
HELIX 249 261 {ECO:0000244|PDB:1DXL}.
STRAND 269 276 {ECO:0000244|PDB:1DXL}.
STRAND 278 291 {ECO:0000244|PDB:1DXL}.
STRAND 295 303 {ECO:0000244|PDB:1DXL}.
STRAND 308 310 {ECO:0000244|PDB:1DXL}.
TURN 318 321 {ECO:0000244|PDB:1DXL}.
STRAND 326 328 {ECO:0000244|PDB:1DXL}.
STRAND 343 345 {ECO:0000244|PDB:1DXL}.
STRAND 350 352 {ECO:0000244|PDB:1DXL}.
HELIX 356 370 {ECO:0000244|PDB:1DXL}.
STRAND 384 386 {ECO:0000244|PDB:1DXL}.
STRAND 388 396 {ECO:0000244|PDB:1DXL}.
HELIX 399 404 {ECO:0000244|PDB:1DXL}.
STRAND 409 415 {ECO:0000244|PDB:1DXL}.
HELIX 416 418 {ECO:0000244|PDB:1DXL}.
HELIX 420 425 {ECO:0000244|PDB:1DXL}.
STRAND 431 437 {ECO:0000244|PDB:1DXL}.
TURN 438 440 {ECO:0000244|PDB:1DXL}.
STRAND 442 450 {ECO:0000244|PDB:1DXL}.
HELIX 453 465 {ECO:0000244|PDB:1DXL}.
HELIX 470 474 {ECO:0000244|PDB:1DXL}.
HELIX 485 495 {ECO:0000244|PDB:1DXL}.
SEQUENCE 501 AA; 53310 MW; 639D2D6368589FCE CRC64;
MAMANLARRK GYSLLSSETL RYSFSLRSRA FASGSDENDV VIIGGGPGGY VAAIKAAQLG
FKTTCIEKRG ALGGTCLNVG CIPSKALLHS SHMYHEAKHS FANHGVKVSN VEIDLAAMMG
QKDKAVSNLT RGIEGLFKKN KVTYVKGYGK FVSPSEISVD TIEGENTVVK GKHIIIATGS
DVKSLPGVTI DEKKIVSSTG ALALSEIPKK LVVIGAGYIG LEMGSVWGRI GSEVTVVEFA
SEIVPTMDAE IRKQFQRSLE KQGMKFKLKT KVVGVDTSGD GVKLTVEPSA GGEQTIIEAD
VVLVSAGRTP FTSGLNLDKI GVETDKLGRI LVNERFSTNV SGVYAIGDVI PGPMLAHKAE
EDGVACVEYL AGKVGHVDYD KVPGVVYTNP EVASVGKTEE QVKETGVEYR VGKFPFMANS
RAKAIDNAEG LVKIIAEKET DKILGVHIMA PNAGELIHEA AIALQYDASS EDIARVCHAH
PTMSEAIKEA AMATYDKPIH I


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