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Database: UniProt
Entry: I5C0M9_9BACT
LinkDB: I5C0M9_9BACT
Original site: I5C0M9_9BACT 
ID   I5C0M9_9BACT            Unreviewed;       423 AA.
AC   I5C0M9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   ORFNames=A3SI_13267 {ECO:0000313|EMBL:EIM75381.1};
OS   Nitritalea halalkaliphila LW7.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Nitritalea.
OX   NCBI_TaxID=1189621 {ECO:0000313|EMBL:EIM75381.1, ECO:0000313|Proteomes:UP000005551};
RN   [1] {ECO:0000313|EMBL:EIM75381.1, ECO:0000313|Proteomes:UP000005551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LW7 {ECO:0000313|EMBL:EIM75381.1,
RC   ECO:0000313|Proteomes:UP000005551};
RA   Jangir P.K., Singh A., Shivaji S., Sharma R.;
RT   "Genome sequence of Nitritalea halalkaliphila LW7.";
RL   Submitted (MAY-2012) 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|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:EIM75381.1}.
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DR   EMBL; AJYA01000030; EIM75381.1; -; Genomic_DNA.
DR   AlphaFoldDB; I5C0M9; -.
DR   STRING; 1189621.A3SI_13267; -.
DR   PATRIC; fig|1189621.3.peg.2762; -.
DR   Proteomes; UP000005551; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
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   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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003692};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005551}.
FT   DOMAIN          2..284
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          304..413
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   423 AA;  45515 MW;  055DE3629F712807 CRC64;
     MNWGCIPTKA LIKSAQVFEY INHAKDYGIK VQDAEVDFTA MVKRSRDVAG GMSKGIQFLF
     KKNKIDQLIG WGRVKPGKKV SVTAEDGAET VYSADHIIIA TGGRARELPA LKIDNEKIIG
     YRKAMVLEDK PKKLVVVGSG AIGVEFAYVY NAIGTEVTIV EFMDRIVPNE DVEVSKALEK
     IYKKNGVKIM TSTEVTGVDT SGEGCKVTVK DKKGNESVIE CDKVLSAVGV VSNVEDIGLE
     DVGILVEKGK IQVDEYYKTN MPGYYAIGDV TPGPALAHVA SAEGIICVEK IAGHHPEALD
     YNNIPGCTYC IPEISSVGYT EAQAKEAGYE LKVGKFPFSA SGKASAAGAK DGFVKLIFDA
     KYGELLGAHM IGANVTEMIA EIVAIRKLET TGMELIKTVH PHPTMSEAVM EAAAAAYDEV
     IHL
//
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