ID L8JUB0_9BACT Unreviewed; 493 AA.
AC L8JUB0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:ELR70877.1};
GN ORFNames=C900_03312 {ECO:0000313|EMBL:ELR70877.1};
OS Fulvivirga imtechensis AK7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Fulvivirga.
OX NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR70877.1, ECO:0000313|Proteomes:UP000011135};
RN [1] {ECO:0000313|EMBL:ELR70877.1, ECO:0000313|Proteomes:UP000011135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK7 {ECO:0000313|EMBL:ELR70877.1,
RC ECO:0000313|Proteomes:UP000011135};
RA Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT "Genome assembly of Fulvivirga imtechensis AK7.";
RL Submitted (DEC-2012) 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:ELR70877.1}.
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DR EMBL; AMZN01000048; ELR70877.1; -; Genomic_DNA.
DR RefSeq; WP_009580676.1; NZ_AMZN01000048.1.
DR AlphaFoldDB; L8JUB0; -.
DR STRING; 1237149.C900_03312; -.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000011135; 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 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; PTHR22912:SF103; DEHYDROGENASE, PUTATIVE-RELATED; 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|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000011135}.
FT DOMAIN 4..327
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 350..458
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 449
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 50
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 276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 493 AA; 54988 MW; B0FDA2FD0304735D CRC64;
MKKYDLVVIG AGPSGYAAAM RAVDFRKKVL LIEKNRVGGA GVTNGALSSK TWWEISRESH
LLRKHLKRFN MDMPEVSFKE VQAEVNRAVE ERKVLLQEHM NLLNSSLFAD LLVFKTGSAR
LLSPNDVEIT SGDVKERVKT DYVILATGSR PRKLPNIPID EKIIMTSDGI EQMEDFPESM
VILGAGVIGC EFATIFSGFG KTKVHLIDKG ERILPFEDED VVRVIERNME NNGVHIHRNA
QLIRMDIVRG RVEYELEYDD GSKEVFNVEK ALVSVGRVPN YEDLWDDNVS IVLTKRGIED
NDTQTSVSNI YAVGDITADI ALVNVGELEG RYAVEKIFGE PRRKLVYENI STIMFLNPEV
AGVGLNEIQA AEKGIAYKVV TLDYACIPRA IAKRNTQGFI KLLVTNDEKM KILGMRVVGN
HASSAIQAVA LLISMDKGIE ELAECVHPHP SITEGIQECV RMLLGKSLFK PDALRGKLSC
RMFTNGEYAD ILF
//
