DLDH_MYCGE
ID DLDH_MYCGE Reviewed; 457 AA.
AC P47513; Q49233;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
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=MG271;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 306-404.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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 -!- 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; L43967; AAC71493.1; -; Genomic_DNA.
DR EMBL; U01784; AAD10605.1; -; Genomic_DNA.
DR PIR; I64229; I64229.
DR RefSeq; WP_009885903.1; NZ_AAGX01000009.1.
DR AlphaFoldDB; P47513; -.
DR SMR; P47513; -.
DR STRING; 243273.MG_271; -.
DR EnsemblBacteria; AAC71493; AAC71493; MG_271.
DR KEGG; mge:MG_271; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_2_14; -.
DR OMA; HMVGDRM; -.
DR OrthoDB; 267896at2; -.
DR BioCyc; MGEN243273:G1GJ2-329-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
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: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 3: Inferred from homology;
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_0000068031"
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"
FT CONFLICT 388..392
FT /note="FVKMM -> LSRWC (in Ref. 2; AAD10605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 50119 MW; 2A0B3F11370AD072 CRC64;
MDYDLIILGA GPAGYIAAEY AGKHKLKTLV IEKQYFGGVC LNVGCIPTKT LLKRAKIIDY
LVHAKDYGIT INGQAKLDWK QLLKQKQEVV DKLVAGVKTI IKGAKVESIE GEATVIDKNK
VQVNNTTYTT NNIIVATGSR PRYLTLPGFE KAQQAGFIID STQALALEGV PKKFVVVGGG
VIGVEFAFLF ASLGSEVTII QGVDRILEVC DSDVSELISK TLKNKGVQII TNAHVVRAEN
NQLFYTVNGV EQSVIGDKIL VSIGRIANTE CLDQLDLKRD HNNKIVLNEK LQTSTTNIYL
IGDVNTQMML AHYAYQQGRY AVDQILNQNQ VKPAEKNKCP ACIYTNPEVA FVGYSEMELQ
KEKIDYVKSS LPFIYSGKAI ADHETNGFVK MMFNPKTGAI LGGCIIASTA SDIIAELALV
MENNLTVFDI ANSISPHPTM NEMVTDVCKK AIFDYFS
