DLDH_DICDI
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 03-AUG-2022, entry version 112.
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 (Slime mold).
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=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + 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.DDB0216232; -.
DR PaxDb; Q54EW8; -.
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; DAKYGEW; -.
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:0045454; P:cell redox homeostasis; IEA:InterPro.
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; -; 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 Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 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
