ID E6N915_CALS0 Unreviewed; 459 AA.
AC E6N915;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN ORFNames=HGMM_F21E09C17 {ECO:0000313|EMBL:BAJ48784.1};
OS Caldiarchaeum subterraneum.
OC Archaea; Nitrososphaerota; Candidatus Caldarchaeales;
OC Candidatus Caldarchaeaceae; Candidatus Caldarchaeum.
OX NCBI_TaxID=311458 {ECO:0000313|EMBL:BAJ48784.1, ECO:0000313|Proteomes:UP000008120};
RN [1] {ECO:0000313|EMBL:BAJ48784.1, ECO:0000313|Proteomes:UP000008120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAJ48784.1, ECO:0000313|Proteomes:UP000008120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21169198; DOI=10.1093/nar/gkq1228;
RA Nunoura T., Takaki Y., Kakuta J., Nishi S., Sugahara J., Kazama H.,
RA Chee G., Hattori M., Kanai A., Atomi H., Takai K., Takami H.;
RT "Insights into the evolution of Archaea and eukaryotic protein modifier
RT systems revealed by the genome of a novel archaeal group.";
RL Nucleic Acids Res. 39:3204-3223(2011).
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}.
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DR EMBL; AP011873; BAJ48784.1; -; Genomic_DNA.
DR AlphaFoldDB; E6N915; -.
DR STRING; 311458.CSUB_C1589; -.
DR Proteomes; UP000008120; 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 NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 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.
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 ECO:0000313|EMBL:BAJ48784.1};
KW Redox-active center {ECO:0000256|RuleBase:RU003692};
KW Reference proteome {ECO:0000313|Proteomes:UP000008120}.
FT DOMAIN 4..320
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 338..444
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 459 AA; 48911 MW; 9AB1A058F2D1835A CRC64;
MKFDAVIVGG GPGGYATAIR LSQLGVKTAL VEKEHLGGEC TNWGCIPSKH LITHAKKIHS
LMELSATGLV TGQMTVNMSK ITASTQQVVQ RLRQGISYLL KTYGVSVYVG EAVLKGSGEV
KVVGEGGSES LEARNIVIAT GTVQSSLSAA PYDGKRIIGF REALYLEVVP KKMLVVGGGA
IGVELGTAYR HLGSDVTVVE LMDQLLPGMD PDAARLLKRG MEKIGVKIHL KTTVEETRYV
DGGVEAVLSN DVKDVFDVVL VVVGKRPSEW VRMLADLGVK LSEKGYVLVD SRMRTSLDGV
YAVGDVTGPP FLAHKAYKQA AVAAENIAGK TVAYDGLVPF GVFTTPEVAA VGLSAETARE
KGYDSAEARF PYAALGRAVA ENEDGFVKLI FDKKTDKVLG ATVVGPHATE TISILTTLIK
LGATVEEASE TIFIHPTYSE AVAEVMHLAH KRSIHYVTR
//
