ID A0A166PX15_9ACTN Unreviewed; 483 AA.
AC A0A166PX15;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:OAA24391.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:OAA24391.1};
GN ORFNames=UG55_103035 {ECO:0000313|EMBL:OAA24391.1};
OS Frankia sp. EI5c.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA24391.1, ECO:0000313|Proteomes:UP000077018};
RN [1] {ECO:0000313|EMBL:OAA24391.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA24391.1,
RC ECO:0000313|Proteomes:UP000077018};
RX PubMed=27389275;
RA D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA Tisa L.S.;
RT "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT Nodules of Elaeagnus angustifolia.";
RL Genome Announc. 4:e00660-16(2016).
RN [2] {ECO:0000313|EMBL:OAA24391.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA24391.1,
RC ECO:0000313|Proteomes:UP000077018};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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:OAA24391.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LRTK01000030; OAA24391.1; -; Genomic_DNA.
DR RefSeq; WP_066069238.1; NZ_LRTK01000030.1.
DR AlphaFoldDB; A0A166PX15; -.
DR STRING; 683316.UG55_103035; -.
DR PATRIC; fig|683316.3.peg.3508; -.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000077018; 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:SF1; NAD(P)H DEHYDROGENASE (QUINONE); 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:OAA24391.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077018}.
FT DOMAIN 3..338
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 359..467
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 195..202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 39..44
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 483 AA; 50198 MW; 440AE5513FCAB1F8 CRC64;
MTRIVILGGG PGGYEAALVA ASLGATATVI DSDGIGGACV LTDCVPSKTL IATSETMTNF
AMAPALGVRP HGDPGVEVGS WDATGRSHLT PPDVVSVDPE QVNERVRALA RAQSADIQSH
LERERVRVVH GTGRLVGPHA VETADGETFV GDVVLVATGA SPREVPGCEP DGERILTWRH
LYELKEIPEH LVVVGSGVTG AEFASAYRAL GAEVTLVSSR ERVLPGEDSD AARVIEDVFV
RRGIQVLNRS RAASVRRIGD GVLVELTDGR AVTGSHALMA VGSVPRTRGL GLTDVGVRLG
SGGHIVVDRM SRTSVPGVYA AGDCTGVLPL ASVAAMQGRI AMWHALGEAV TPLRLGTVSS
NIFTEPEIAT VGVTQRMKDS GAIAAEVTTV PLARNPRAKM MGISDGFVKL FCRPGSGSVL
GGVIVAPRAS ELILSISLAV ENGLTVDQIA HTFSIYPSLS GSITEAARVL RPRDLFAGFD
TPA
//
