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Database: UniProt
Entry: A0A0J1H1E1_9GAMM
LinkDB: A0A0J1H1E1_9GAMM
Original site: A0A0J1H1E1_9GAMM 
ID   A0A0J1H1E1_9GAMM        Unreviewed;       483 AA.
AC   A0A0J1H1E1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:KLV05643.1};
DE            EC=1.8.1.4 {ECO:0000313|EMBL:KLV05643.1};
GN   ORFNames=ABT57_20715 {ECO:0000313|EMBL:KLV05643.1};
OS   Photobacterium ganghwense.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV05643.1, ECO:0000313|Proteomes:UP000035909};
RN   [1] {ECO:0000313|EMBL:KLV05643.1, ECO:0000313|Proteomes:UP000035909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV05643.1,
RC   ECO:0000313|Proteomes:UP000035909};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) 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:KLV05643.1}.
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DR   EMBL; LDOU01000024; KLV05643.1; -; Genomic_DNA.
DR   RefSeq; WP_047887165.1; NZ_PYMI01000006.1.
DR   AlphaFoldDB; A0A0J1H1E1; -.
DR   STRING; 320778.ABT57_20715; -.
DR   PATRIC; fig|320778.3.peg.4453; -.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000035909; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   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; 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:KLV05643.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035909}.
FT   DOMAIN          7..326
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          349..458
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        448
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         142..144
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         179..186
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        43..48
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   483 AA;  52668 MW;  C0F1B6F7492D9B51 CRC64;
     MKTLNVDVAV IGGGTAGLGA YRAAKAHTPH VVMIEGGPYG TTCARVGCMP SKLLIAAAES
     VHQIEKAPAF GVYPQGEIHI NGREVMDRVK RERDRFVGFV LEGVDEIPAE DKIAGYAKFI
     DNNTLQVDDH TLIHAERIVI ATGSRPAYPA VWNELGDRLI INDDVFEWDD LPQSVAVFGP
     GVIGLELGQA LKRLGVEVVM FGLGGQVGPL TDPAIMAYAD KAFNEEFYLD ADVKVESMKR
     IGDSVEIQYL NKEGVLDTIT VDYVLAATGR RPNVDKLAIE NTDLELDQRG VPMADYYTLQ
     TSVASIFIAG DASNQLPLLH EAADQGRIAG DNAGRFPDIR AGLRRSKISA VFSDPQIAMV
     GETYREISNR LGNCGCFETG EVSFENQGRS RVMLRNKGML HVYGEHGTGR FLGAEMMGPN
     AEHLAHLLAW AHQNKMTIAQ MLDMPFYHPV IEEGVRTALR DLNAKLHLGP EMIKHCLDCG
     PGC
//
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