ID A0A0T5P9E7_9RHOB Unreviewed; 464 AA.
AC A0A0T5P9E7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN Name=lpd_2 {ECO:0000313|EMBL:QEW27290.1};
GN ORFNames=RIdsm_03102 {ECO:0000313|EMBL:QEW27290.1}, XM52_10070
GN {ECO:0000313|EMBL:KRS17899.1};
OS Roseovarius indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS17899.1, ECO:0000313|Proteomes:UP000051401};
RN [1] {ECO:0000313|EMBL:KRS17899.1, ECO:0000313|Proteomes:UP000051401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B108 {ECO:0000313|EMBL:KRS17899.1,
RC ECO:0000313|Proteomes:UP000051401};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius indicus B108T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEW27290.1, ECO:0000313|Proteomes:UP000325785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW27290.1,
RC ECO:0000313|Proteomes:UP000325785};
RA Vollmers J., Petersen J.;
RT "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT geographic distances.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00043836,
CC ECO:0000256|RuleBase:RU003692};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC ECO:0000256|RuleBase:RU003692};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC ECO:0000256|RuleBase:RU003692};
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000256|RuleBase:RU003692}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003692}.
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DR EMBL; LAXI01000005; KRS17899.1; -; Genomic_DNA.
DR EMBL; CP031598; QEW27290.1; -; Genomic_DNA.
DR RefSeq; WP_057815856.1; NZ_LAXI01000005.1.
DR AlphaFoldDB; A0A0T5P9E7; -.
DR STRING; 540747.SAMN04488031_101243; -.
DR KEGG; rid:RIdsm_03102; -.
DR PATRIC; fig|540747.5.peg.4939; -.
DR OrthoDB; 9776382at2; -.
DR Proteomes; UP000051401; Unassembled WGS sequence.
DR Proteomes; UP000325785; 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 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003692}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003692};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003692};
KW Reference proteome {ECO:0000313|Proteomes:UP000051401}.
FT DOMAIN 6..325
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 345..453
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 180..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 464 AA; 49827 MW; F1BF8510EB830D78 CRC64;
MAAKSFDMIV IGAGPGGYVA AIRGAQLGLN VAIVEREHMG GICLNWGCIP TKAMLRSSEV
FHLMHRAKEF GLKADGIDYD LDAVVKRSRG VAKQLASGVG HLMKKNKITT VMGEATLPSK
GKVSVKTEKG TEELESKAIV LATGARAREL PGLEADGDLV WTYKHALLPP RMPKKLLVIG
SGAIGIEFAS FYNTLGADTT VVEVMDRILP VEDAEISAFA KKAFQKQKMK IMEKATVKKL
DRAKGKVTAH IETGGKTETH EFDTVISAVG IVGNVEGLGL EDLGVKVDRT HVIVDEYCRT
GVDGLYAIGD LAGAPWLAHK ASHEGVMVAE LIAGGHPHPV RPDSIAGCTY CHPQIASVGM
TEAQAKEKGY KIKVGRFPFI GNGKAIALGE AEGMMKTVFD EKTGELLGAH MVGAEVTELI
QGYVVGRQLE TTEEDLMHAV FPHPTLSEMM HETVLDAYDR VIHI
//
