ID A0A1B6Z4E4_9SPHN Unreviewed; 460 AA.
AC A0A1B6Z4E4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:OAN98312.1};
GN ORFNames=A8B75_19815 {ECO:0000313|EMBL:OAN98312.1};
OS Sphingomonadales bacterium EhC05.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX NCBI_TaxID=1849171 {ECO:0000313|EMBL:OAN98312.1, ECO:0000313|Proteomes:UP000078455};
RN [1] {ECO:0000313|Proteomes:UP000078455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC05 {ECO:0000313|Proteomes:UP000078455};
RA Rosana A., Orata F., Boucher Y., Case R.;
RL Submitted (MAY-2016) 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}.
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:OAN98312.1}.
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DR EMBL; LXYP01000059; OAN98312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6Z4E4; -.
DR STRING; 1849171.A8B75_19815; -.
DR Proteomes; UP000078455; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
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; IPR036324; Mn/Fe_SOD_N_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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000078455}.
FT DOMAIN 1..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 329..435
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 124..126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 161..168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 26..31
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 460 AA; 49581 MW; 38B60E65EBC7BC56 CRC64;
MAAYREASQY SDRVALIDGG PLGTTCARVG CMPSKLLIAA AEAAHAGSRT PMFGVRYDDP
AIDGIAVMKR VRSERDRFVG FVTEAVHGFD KGEIIREYAR FEDDHTLRLT SGRKISARTI
VIATGSRPAI PQALFAAGER LIVNDDIFDW ADLPGSVAVF GAGVIGLELD QALHRLGVRV
RLFGRGGQAG PLTDPVVRQY ATDIFSGEFP AIWNADTRIS RKGETVAVRW GETADQEASF
DYLVAATGRR PNIDKIGLEN SGLPLGKTGV PQYDPLSGRV GDTHIFIAGD AALDLPLLHE
AADEGRLAGE NAARFPHSYK RSRRTPIGIV FSDPQIAMVG ASHASHLARQ GCHFATGEVS
FEDQGRARVM GLNKGVLRLY AEHGSARFLG AEMIGPLAEH IAHLLAWSIQ ANMTVEQILQ
MPFYHPVLEE GVRTAFRNLN HALGFGPNPP LGCIDCGPGA
//
