ID DLDH_ZYMMO Reviewed; 466 AA.
AC P50970; P96191; Q5NQ69;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes;
GN Name=lpd; OrderedLocusNames=ZMO0512;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RA Bringer-Meyer S., Neveling U., Klasen R., Sahm H.;
RT "Cloning, sequencing and expression of the Zymomonas mobilis
RT dihydrolipoamide dehydrogenase gene (lpd) in Escherichia coli.";
RL (In) Bisswanger H., Schellenberger A. (eds.);
RL Biochemistry and physiology of thiamin diphosphate enzymes, pp.382-389,
RL Intemann, Germany (1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RX PubMed=9515924; DOI=10.1128/jb.180.6.1540-1548.1998;
RA Neveling U., Klasen R., Bringer-Meyer S., Sahm H.;
RT "Purification of the pyruvate dehydrogenase multienzyme complex of
RT Zymomonas mobilis and identification and sequence analysis of the
RT corresponding genes.";
RL J. Bacteriol. 180:1540-1548(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid
CC dehydrogenase complexes. {ECO:0000250}.
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 -!- 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; X82291; CAA57734.1; -; Genomic_DNA.
DR EMBL; X93605; CAA63810.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89136.1; -; Genomic_DNA.
DR PIR; S57635; S57635.
DR RefSeq; WP_011240416.1; NZ_CP035711.1.
DR AlphaFoldDB; P50970; -.
DR SMR; P50970; -.
DR STRING; 264203.ZMO0512; -.
DR KEGG; zmo:ZMO0512; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_2_5; -.
DR BRENDA; 1.8.1.4; 6765.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 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 Cytoplasm; Disulfide bond; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..466
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068054"
FT ACT_SITE 445
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 34..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 180..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 92
FT /note="T -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="L -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="F -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="A -> D (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="Q -> H (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 49746 MW; CDAB257276BBD319 CRC64;
MADHFDLIVL GGGPGGYVAA IRAAQLNLKV ALVERVHLGG ICLNWGCIPT KSLLRSAEVY
HEMQNAEAYG LTSFKPDFDL DKIIARSREV ATRLASGVKT LLRKNKVEVI SGVGQLTGNQ
QMLVETTEGE EKILEAKDII IATGARARQL PNVHSDGKHI WTYHHALKPP AMPKKLLVIG
SGAIGIEFAS FYADFGAEVS IVEHAPQILP MEDAEVSAYV AKAFKKRGIR ILTQSALQNL
TPDDEGVTAE IAGADGKVTK ERFSHAIVAI GVVANVENIG LDKLGIKLDR GFIAVDGFGR
TNVDHVWAIG DVAGAPCLAH KASHQGVIAA EAIAGCDHVH PLNTQNIPGC TYARPQVASV
GLTEEKARQQ GYNVKIGNFP FIANGKAIAQ GATDGFVKTV FDADSGALLG AHMVGAEVTE
MIQGYTVART LETTEAEIME TIFPHPTLSE AMHESVLAAY GRALHF
//
