ID   DLDH_DICDI              Reviewed;         488 AA.
AC   Q54EW8; Q6S4V6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 118.
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   Flags: Precursor;
GN   Name=lpd; Synonyms=bkdD, dld, odhC, pdhD; ORFNames=DDB_G0291648;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-357.
RX   PubMed=15003488; DOI=10.1016/j.ijpara.2003.11.025;
RA   Huang J., Mullapudi N., Sicheritz-Ponten T., Kissinger J.C.;
RT   "A first glimpse into the pattern and scale of gene transfer in
RT   Apicomplexa.";
RL   Int. J. Parasitol. 34:265-274(2004).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AAFI02000177; EAL61808.1; -; Genomic_DNA.
DR   EMBL; AY466389; AAS47709.1; -; Genomic_DNA.
DR   RefSeq; XP_635122.1; XM_630030.1.
DR   AlphaFoldDB; Q54EW8; -.
DR   SMR; Q54EW8; -.
DR   STRING; 44689.Q54EW8; -.
DR   PaxDb; 44689-DDB0216232; -.
DR   EnsemblProtists; EAL61808; EAL61808; DDB_G0291648.
DR   GeneID; 8628069; -.
DR   KEGG; ddi:DDB_G0291648; -.
DR   dictyBase; DDB_G0291648; lpd.
DR   eggNOG; KOG1335; Eukaryota.
DR   HOGENOM; CLU_016755_0_1_1; -.
DR   InParanoid; Q54EW8; -.
DR   OMA; CAQLGMK; -.
DR   PhylomeDB; Q54EW8; -.
DR   Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-DDI-6783984; Glycine degradation.
DR   Reactome; R-DDI-70268; Pyruvate metabolism.
DR   Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR   Reactome; R-DDI-71064; Lysine catabolism.
DR   Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR   PRO; PR:Q54EW8; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:dictyBase.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISS:dictyBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; ISS:dictyBase.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0006546; P:glycine catabolic process; ISS:dictyBase.
DR   GO; GO:0006550; P:isoleucine catabolic process; ISS:dictyBase.
DR   GO; GO:0006564; P:L-serine biosynthetic process; ISS:dictyBase.
DR   GO; GO:0006552; P:leucine catabolic process; ISS:dictyBase.
DR   GO; GO:0006574; P:valine catabolic process; ISS:dictyBase.
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:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase;
KW   Redox-active center; Reference proteome; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..488
FT                   /note="Dihydrolipoyl dehydrogenase, mitochondrial"
FT                   /id="PRO_0000327450"
FT   ACT_SITE        467
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         52..61
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         163..165
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..207
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         341..344
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..66
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   488 AA;  51794 MW;  A7DD67E8F7707783 CRC64;
     MLRINRISNL RTFGQRFFST EQQDVVVIGG GPGGYVAGIK AGQLGMKVTV VEKRGKLGGT
     CLNVGCIPSK ALLNASHLYE EATTKMSKYG VKCSGVELDL GAMMQYKDKS VSGLTSGIEG
     LFKKNKVKYD KGFGKITGPN TVEVTLNDGS VKTIETKNIV IATGSEVTSL PNVNIDEESI
     ISSTGALALK SVPKKLIVIG GGVIGLELGS VWSRLGSETT VVEFTNRIAA GADGEVAKKF
     QKSLEKQHMK FHLETKVTSV VKKSDGKVTV TVEQVGAGGF TGTLEADAVL VSVGRRPNTS
     GLGLESVGIP TDKAGRVEVG DHFNTKVPSI FAIGDAIRGP MLAHKAEEEG IAIIEQIHNG
     GGHVNYGAIP SIIYTHPEVA WVGKTEEELQ KEGIQYNIGR FPFVANSRAK TNDDVEGFVK
     FLAAKDSDRV LGAHIMGTNA GELIGECVLA MEYGASCEDI ARTCHGHPTL SEAVKEAAMD
     AYDKPIHM
//