ID A0A0F7KPP8_9SPHN Unreviewed; 475 AA.
AC A0A0F7KPP8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:MBB5731275.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:AKH42498.1, ECO:0000313|EMBL:MBB5731275.1};
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:AKH42498.1};
GN Name=lpd_2 {ECO:0000313|EMBL:AKH42498.1};
GN ORFNames=FHS61_000268 {ECO:0000313|EMBL:MBB5731275.1}, WYH_01458
GN {ECO:0000313|EMBL:AKH42498.1};
OS Croceibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH42498.1, ECO:0000313|Proteomes:UP000034392};
RN [1] {ECO:0000313|EMBL:AKH42498.1, ECO:0000313|Proteomes:UP000034392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26DY36 {ECO:0000313|EMBL:AKH42498.1,
RC ECO:0000313|Proteomes:UP000034392};
RA Wu Y.-H., Cheng H., Wu X.-W.;
RT "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5731275.1, ECO:0000313|Proteomes:UP000556014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100738 {ECO:0000313|EMBL:MBB5731275.1,
RC ECO:0000313|Proteomes:UP000556014};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; CP011452; AKH42498.1; -; Genomic_DNA.
DR EMBL; JACIJL010000001; MBB5731275.1; -; Genomic_DNA.
DR RefSeq; WP_046903301.1; NZ_JACIJL010000001.1.
DR AlphaFoldDB; A0A0F7KPP8; -.
DR STRING; 1267766.WYH_01458; -.
DR KEGG; aay:WYH_01458; -.
DR PATRIC; fig|1267766.3.peg.1468; -.
DR OrthoDB; 7410809at2; -.
DR Proteomes; UP000034392; Chromosome.
DR Proteomes; UP000556014; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 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|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000313|EMBL:AKH42498.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034392}.
FT DOMAIN 13..328
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 351..451
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 441
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 147..149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 184..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 271
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 DISULFID 49..54
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 475 AA; 50042 MW; 3E281FCCF9DB2B75 CRC64;
MAENASGHTH RCDVAVIGAG TAGLAAERAA RRNGASTLLI DPEFNGTTCA NVGCMPSKLL
IAAAREAHRI GQADLFGIEI ADMRVDGPAI MQRVRSERDR FAGFTREKIG NLPEGVTIRA
RARFDGPDRL LLDNGDVVEA RAIVIATGSA PALPPPFAEL GDLAITSDGV FELKDLPGSL
AVVGSGAIGL ELAQAFARLG VEVALFDRGE TMGKIRCPRV HAALRDIIEA DMDLHLGVDV
KPESADGRVK LRWSGKEEGT AEFDKVLVAV GRPPVLDTLD LERSGLELDE YGVPRHDRAT
MRCGDSAIFI AGDVAADLPL LHEASHDGAI AGRNAAALPA PIRTDRHVAF SIIFTEPAIA
SIGKSEDDGA VTGTADFSDQ GRARVEGRNQ GRLTLYAAAP DGRLIGADMA APAGEHLAHL
LCWAIQQGLT ATQLLEMPFY HPTIEEGLKQ ALRTICAATP IDLPADQDTG APPGA
//
