ID   A0A7W9R6G7_9SPHN        Unreviewed;       466 AA.
AC   A0A7W9R6G7;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   29-SEP-2021, entry version 2.
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   ORFNames=HNP60_000039 {ECO:0000313|EMBL:MBB5984065.1};
OS   Sphingobium sp. B1D3A.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=2735886 {ECO:0000313|EMBL:MBB5984065.1, ECO:0000313|Proteomes:UP000568488};
RN   [1] {ECO:0000313|EMBL:MBB5984065.1, ECO:0000313|Proteomes:UP000568488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1D3A {ECO:0000313|EMBL:MBB5984065.1,
RC   ECO:0000313|Proteomes:UP000568488};
RA   Elkins J.;
RT   "Exploring microbial biodiversity for novel pathways involved in the
RT   catabolism of aromatic compounds derived from lignin.";
RL   Submitted (AUG-2020) 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|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {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:MBB5984065.1}.
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DR   EMBL; JACHKA010000001; MBB5984065.1; -; Genomic_DNA.
DR   Proteomes; UP000568488; Unassembled WGS sequence.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003692};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003692}.
FT   DOMAIN          7..329
FT                   /note="Pyr_redox_2"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          348..456
FT                   /note="Pyr_redox_dim"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   466 AA;  48484 MW;  6FA390F1A47968EC CRC64;
     MADQFDYDVL VIGAGPGGYV AAIRAAQLGL KTACAESRET LGGTCLNVGC IPSKALLHAS
     EYFEAAAGGK MAAMGIKVKP ELDLATMQGQ RVDAVKGLTG GVEFLFRKNK VDWLKGLATF
     KDAHSVEVAG KTVTAKNIVI ATGSSVTPLP GVAVDNAKGV IVDSTGALEL DKVPGHLVVI
     GGGVIGLELG SVWRRLGAKV TVVEYLDQIL PGMDSDVRKE ANKIFRKQGI EFRLETKVTG
     ATVKGKKATL TLEPAAGGEA EKLEADVVLV AIGRRANTEG LGLDKIGLAL NQRGQIETDH
     DFATKVPGVW AIGDVIPGPM LAHKAEDEGI AVAENIAGLT GIVNHDVIPS VVYTQPEIAG
     VGLTEEAAKA KGSVKVGKFP MLANSRAKTN HEPDGFVKVI ADAETDRVLG VWIVASVAGT
     MIAQAAQAME FGATSEDIAY TCHAHPTHSE AVKEAAMAVL GKPIHV
//