ID DLDH_PEA Reviewed; 501 AA.
AC P31023;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 24-JAN-2024, entry version 147.
DE RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=Glycine cleavage system L protein;
DE AltName: Full=Pyruvate dehydrogenase complex E3 subunit;
DE Short=E3;
DE Short=PDC-E3;
DE Flags: Precursor;
GN Name=LPD;
OS Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=1541297; DOI=10.1111/j.1432-1033.1992.tb16706.x;
RA Bourguignon J., Macherel D., Neuburger M., Douce R.;
RT "Isolation, characterization, and sequence analysis of a cDNA clone
RT encoding L-protein, the dihydrolipoamide dehydrogenase component of the
RT glycine cleavage system from pea-leaf mitochondria.";
RL Eur. J. Biochem. 204:865-873(1992).
RN [2]
RP SEQUENCE REVISION TO 480.
RA Bourguignon J.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Birte; TISSUE=Leaf;
RX PubMed=1560008; DOI=10.1016/s0021-9258(18)42577-x;
RA Turner S.R., Ireland R., Rawsthorne S.;
RT "Purification and primary amino acid sequence of the L subunit of glycine
RT decarboxylase. Evidence for a single lipoamide dehydrogenase in plant
RT mitochondria.";
RL J. Biol. Chem. 267:7745-7750(1992).
RN [4]
RP SEQUENCE REVISION TO 499-501.
RA Rawsthorne S.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 32-61 AND 493-501, AND MASS SPECTROMETRY.
RX PubMed=8546688; DOI=10.1042/bj3130229;
RA Bourguignon J., Merand V., Rawsthorne S., Forest E., Douce R.;
RT "Glycine decarboxylase and pyruvate dehydrogenase complexes share the same
RT dihydrolipoamide dehydrogenase in pea leaf mitochondria: evidence from mass
RT spectrometry and primary-structure analysis.";
RL Biochem. J. 313:229-234(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 32-501 IN COMPLEX WITH FAD,
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=10806386; DOI=10.1046/j.1432-1033.2000.01330.x;
RA Faure M., Bourguignon J., Neuburger M., MacHerel D., Sieker L., Ober R.,
RA Kahn R., Cohen-Addad C., Douce R.;
RT "Interaction between the lipoamide-containing H-protein and the lipoamide
RT dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system
RT 2. Crystal structures of H- and L-proteins.";
RL Eur. J. Biochem. 267:2890-2898(2000).
RN [7]
RP ERRATUM OF PUBMED:10806386.
RA Faure M., Bourguignon J., Neuburger M., MacHerel D., Sieker L., Ober R.,
RA Kahn R., Cohen-Addad C., Douce R.;
RL Eur. J. Biochem. 267:3914-3914(2000).
CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
CC cleavage system as well as of the alpha-ketoacid dehydrogenase
CC complexes. The pyruvate dehydrogenase complex contains multiple copies
CC of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) +
CC N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10806386}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- MASS SPECTROMETRY: Mass=49753; Mass_error=5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8546688};
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X63464; CAA45066.2; -; mRNA.
DR EMBL; X62995; CAA44729.1; -; mRNA.
DR PIR; S22384; S22384.
DR PDB; 1DXL; X-ray; 3.15 A; A/B/C/D=32-501.
DR PDBsum; 1DXL; -.
DR AlphaFoldDB; P31023; -.
DR SMR; P31023; -.
DR IntAct; P31023; 1.
DR EnsemblPlants; Psat0s2692g0120.1; Psat0s2692g0120.1.cds; Psat0s2692g0120.
DR Gramene; Psat0s2692g0120.1; Psat0s2692g0120.1.cds; Psat0s2692g0120.
DR BRENDA; 1.2.1.104; 4872.
DR BRENDA; 1.4.1.27; 4872.
DR SABIO-RK; P31023; -.
DR EvolutionaryTrace; P31023; -.
DR GO; GO:0005960; C:glycine cleavage complex; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IDA:CACAO.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR22912:SF220; LEGHEMOGLOBIN REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Mitochondrion; NAD; Oxidoreductase; Redox-active center; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8546688"
FT CHAIN 32..501
FT /note="Dihydrolipoyl dehydrogenase, mitochondrial"
FT /id="PRO_0000030299"
FT ACT_SITE 480
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 67..76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10806386"
FT BINDING 85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10806386"
FT BINDING 178..180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 215..222
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10806386"
FT BINDING 354..357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10806386"
FT DISULFID 76..81
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:10806386"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 115..140
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 278..291
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1DXL"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 388..396
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 420..425
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:1DXL"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:1DXL"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 453..465
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 470..474
FT /evidence="ECO:0007829|PDB:1DXL"
FT HELIX 485..495
FT /evidence="ECO:0007829|PDB:1DXL"
SQ 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
//
