ID   A0A176F3B2_9RHOB        Unreviewed;       473 AA.
AC   A0A176F3B2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:KZY33863.1};
GN   ORFNames=A3731_19845 {ECO:0000313|EMBL:KZY33863.1};
OS   Roseovarius sp. HI0049.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1822235 {ECO:0000313|EMBL:KZY33863.1, ECO:0000313|Proteomes:UP000077043};
RN   [1] {ECO:0000313|EMBL:KZY33863.1, ECO:0000313|Proteomes:UP000077043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0049 {ECO:0000313|EMBL:KZY33863.1,
RC   ECO:0000313|Proteomes:UP000077043};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KZY33863.1}.
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DR   EMBL; LWFA01002922; KZY33863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176F3B2; -.
DR   Proteomes; UP000077043; 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; 3.
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; 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   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   4: Predicted;
FT   DOMAIN          7..317
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          341..441
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   REGION          449..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  49832 MW;  2451EA4750BC7335 CRC64;
     MTRHVADVAV IGAGTAGLAA ERHARGQGAQ TRLIDPAFAG TTCATVGCMP SKLLIAAADA
     AHGAADADRF GIHAKVQVNG PEVFDRVRRM RDDFARGVRQ SIADLPDGTC LKARARFDAP
     GILALDTGDI IEARAIVIAT GAAPNLPGPY RAVSDRVLTN RTIFELDELP NSLGVIGAGP
     LGLELAQAMH RLGVEVEVFD SGESLAGLPP ETSRALYATL SDSFPIHLNC KPDPAPHPDG
     VELSWPGHTA RFERILVAAG RPPSLDALEL ENADLDLDDH GTPIFDPRTL QCGDAPVFIA
     GDANHDRPLL HEASDEGTIA GSNAATWPDV AQSPRKIPLS ISFTRPEAAT IGTIPDPDDD
     SHVTGTADYA DQGRAKVIGQ AHGLLRLHAT TDGQLTGASL CAPGGEHLAH MLAWAIQCGL
     TAPEVLDLPF YHPTLAEGLQ PALRDICRQT ERTKPWHRDD DPRPGSDGGA PDA
//