ID A0A5N7UU76_9FLAO Unreviewed; 467 AA. AC A0A5N7UU76; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 22-FEB-2023, entry version 7. DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692}; DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692}; GN Name=lpdA {ECO:0000313|EMBL:MPS72299.1}; GN ORFNames=E2590_04025 {ECO:0000313|EMBL:MPS72299.1}; OS Chryseobacterium sp. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae; OC Chryseobacterium group; Chryseobacterium. OX NCBI_TaxID=1871047 {ECO:0000313|EMBL:MPS72299.1, ECO:0000313|Proteomes:UP000326538}; RN [1] {ECO:0000313|EMBL:MPS72299.1, ECO:0000313|Proteomes:UP000326538} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RQ_Bin_10 {ECO:0000313|EMBL:MPS72299.1}; RA Farkas C., Perez-Pantoja D.; RT "activated sludge metagenome from Chilean kraft pulp-mill effluents with RT ten lignin monomers as a carbon source."; RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases. 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 Evidence={ECO:0000256|ARBA:ARBA00001492, 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MPS72299.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; SPFE01000003; MPS72299.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5N7UU76; -. DR Proteomes; UP000326538; Unassembled WGS sequence. 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 PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE; 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 TIGRFAMs; TIGR01350; lipoamide_DH; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692}; KW Flavoprotein {ECO:0000256|RuleBase:RU003692}; KW NAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003692, KW ECO:0000313|EMBL:MPS72299.1}; KW Redox-active center {ECO:0000256|RuleBase:RU003692}. FT DOMAIN 4..328 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 347..455 FT /note="Pyridine nucleotide-disulphide oxidoreductase FT dimerisation" FT /evidence="ECO:0000259|Pfam:PF02852" FT ACT_SITE 445 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2" FT BINDING 51 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 115 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 144..146 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 181..188 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 204 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 272 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 313 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 319..322 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT DISULFID 42..47 FT /note="Redox-active" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4" SQ SEQUENCE 467 AA; 50792 MW; 9FC56D31764DC1C0 CRC64; METFDITVIG SGPGGYVAAI RSAQLGYKTA IIEKYNTLGG TCTNVGCIPT KALLDSTHHY ADALNSFGVH GIEYSDLRLN FEQLIKRKSE VVTKNTQGLD FLMRKNKITV FHGSGSFVNN ETLKILHDDQ SETIINSDKF IIATGSKPAT IPGVTIDKKR IITSTEALAL QENPESIVII GGGVIGVEMA SIFNRIGTKV TILEYADNLI ANMDSELGRT LMKILTKEGI EIKLQQAVYK AENLGSTAKV FSRNKQGEEQ ELTADYILVA VGRKPYIKGL GLENTNVELN ANGTIKVNEL LQTTAPNIYA IGDVIGGAML AHKAEEEAVF VVERINGQKP HINYGRIPSV VYTWPEVAYV GATEEELRKQ EVEYNIGKFP FAVNARARAG METEGFVKVL SDPKYGELLG VHIIGARAAD LIAQAVVGLE YEVTANDMAS ISYAHPTYSE VLKEAYTIAS GRPSLNI //