DLDH_MYCPN
ID DLDH_MYCPN Reviewed; 457 AA.
AC P75393;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of pyruvate complex;
GN Name=pdhD; OrderedLocusNames=MPN_390; ORFNames=MP448;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid
CC dehydrogenase complexes. {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P75393; P00747: PLG; Xeno; NbExp=3; IntAct=EBI-2259617, EBI-999394;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; U00089; AAB96096.1; -; Genomic_DNA.
DR PIR; S73774; S73774.
DR RefSeq; NP_110078.1; NC_000912.1.
DR RefSeq; WP_010874746.1; NC_000912.1.
DR AlphaFoldDB; P75393; -.
DR SMR; P75393; -.
DR IntAct; P75393; 3.
DR STRING; 272634.MPN_390; -.
DR EnsemblBacteria; AAB96096; AAB96096; MPN_390.
DR KEGG; mpn:MPN_390; -.
DR PATRIC; fig|272634.6.peg.421; -.
DR HOGENOM; CLU_016755_0_2_14; -.
DR OMA; HMVGDRM; -.
DR BioCyc; MetaCyc:MON-585; -.
DR BioCyc; MPNE272634:G1GJ3-617-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..457
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068032"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 32..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 178..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 262..265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 40..45
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 457 AA; 49437 MW; EB044FD676F3F28E CRC64;
MNYDLIIIGA GPAGYVAAEY AGKHKLKTLV VEKEYFGGVC LNVGCIPTKT LLKRAKIVDY
LRHAQDYGIS INGQVALNWN QLLEQKGKVV SKLVGGVKAI IASAKAETVM GEAKVLDPNT
VEVAGKTYTT KSIVVATGSR PRYLTLPGFA EARQNGFVID STQALSLEGV PRKLVVVGGG
VIGIEFAFLY ASLGSEVTIL QGVDRILEIF DTEVSDLVAK LLQTKNVKII TNAQVTRANN
NEVFYSQNGQ EGSVVGDRIL VSIGRIPNTE CLDGLNLQRD ERNRIVLNQD LQTSIPNIYI
VGDANAQLML AHFAYQQGRY AVNHILNKKQ VKPAQKLTCP SCIYTNPEVA SVGYTEMELK
KQGIPYVKTN LVLAHCGKAI ADNETNGFVK MMFDPQTGKI LGCCIIAATA SDMIAELALA
MGAGLTVFDI ANSISPHPTI NEMIADVCKK ALFDHFK
