ID Q5LRA7_RUEPO Unreviewed; 464 AA. AC Q5LRA7; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 125. 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 OrderedLocusNames=SPO2222 {ECO:0000313|EMBL:AAV95488.1}; OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter OS pomeroyi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Ruegeria. OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV95488.1, ECO:0000313|Proteomes:UP000001023}; RN [1] {ECO:0000313|EMBL:AAV95488.1, ECO:0000313|Proteomes:UP000001023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3 RC {ECO:0000313|Proteomes:UP000001023}; RX PubMed=15602564; DOI=10.1038/nature03170; RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L., RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M., RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.; RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine RT environment."; RL Nature 432:910-913(2004). RN [2] {ECO:0000313|EMBL:AAV95488.1, ECO:0000313|Proteomes:UP000001023} RP GENOME REANNOTATION. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3 RC {ECO:0000313|Proteomes:UP000001023}; RX PubMed=25780504; DOI=10.1186/1944-3277-9-11; RA Rivers A.R., Smith C.B., Moran M.A.; RT "An updated genome annotation for the model marine bacterium Ruegeria RT pomeroyi DSS-3."; RL Stand. Genomic Sci. 9:11-11(2014). 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}. 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; CP000031; AAV95488.1; -; Genomic_DNA. DR RefSeq; WP_011047944.1; NC_003911.12. DR AlphaFoldDB; Q5LRA7; -. DR STRING; 246200.SPO2222; -. DR PaxDb; 246200-SPO2222; -. DR KEGG; sil:SPO2222; -. DR eggNOG; COG1249; Bacteria. DR HOGENOM; CLU_016755_0_2_5; -. DR OrthoDB; 9776382at2; -. DR Proteomes; UP000001023; Chromosome. DR GO; GO:0045250; C:cytosolic pyruvate dehydrogenase complex; TAS:TIGR. 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:0006086; P:acetyl-CoA biosynthetic process from pyruvate; TAS:TIGR. 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}; Pyruvate {ECO:0000313|EMBL:AAV95488.1}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, KW ECO:0000256|RuleBase:RU003692}; KW Reference proteome {ECO:0000313|Proteomes:UP000001023}. 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; 49696 MW; 590944C589FBCDA7 CRC64; MAAQSYDVIV IGAGPGGYVA AIRAAQLGLK ACVVEREHLG GICLNWGCIP TKALLRSSEV FHLMERAKEF GLKADNIGYD LDAVVKRSRG VAKQLSGGIG HLMKKNKIDV VMGEATIPAK GKVSVKTDKG TQELTAKNII LATGARAREL PGLEADGDLV WTYKHALQPV RMPKKLLVIG SGAIGIEFAS FYNTLGADTT VVEVMDRVLP VEDAEISAFA KKSFVKQGMK IMEKSMVKQL DRAKGKVTAH IETGGKVEKL EFDTVISAVG IVGNVENLGL EALGVKIDRT HVVTDAYCRT GVEGLYAIGD IAGAPWLAHK ASHEGVMVAE LIAGKHAHPV KPESIAGCTY CHPQVASVGY TEAKAKELGY DIKVGRFPFI GNGKAIALGE VEGMIKTIFD AKTGELLGAH MVGAEVTEMI QGYVVGRQLE TTEEDLMHTV FPHPTLSEMM HESVLDAYGR VIHM //