ID A0A316C494_PSESE Unreviewed; 473 AA.
AC A0A316C494;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide dehydrogenase (E3) component {ECO:0000313|EMBL:PWJ84113.1};
GN ORFNames=C7441_10626 {ECO:0000313|EMBL:PWJ84113.1};
OS Pseudaminobacter salicylatoxidans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Pseudaminobacter.
OX NCBI_TaxID=93369 {ECO:0000313|EMBL:PWJ84113.1, ECO:0000313|Proteomes:UP000245396};
RN [1] {ECO:0000313|EMBL:PWJ84113.1, ECO:0000313|Proteomes:UP000245396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6986 {ECO:0000313|EMBL:PWJ84113.1,
RC ECO:0000313|Proteomes:UP000245396};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWJ84113.1}.
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DR EMBL; QGGG01000006; PWJ84113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316C494; -.
DR STRING; 1192868.GCA_000304395_03163; -.
DR OrthoDB; 9781772at2; -.
DR Proteomes; UP000245396; 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; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 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 Pyruvate {ECO:0000313|EMBL:PWJ84113.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245396}.
FT DOMAIN 8..321
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 341..448
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 141..143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 178..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 473 AA; 50474 MW; 426B16D94B930B80 CRC64;
MARTLTPDIC IIGAGAAGLS AAAAAVTYGA SVVLVEKSRM GGNHLHHGCI PSKALIAASR
HAHAPQSGPP FGIGATQPDV DFAAVRQHIR DTIATLAPNN SAEHFTAFGV EVIKAEGRFA
DGQTLLAGDA TVRARRFVIA TGSVPVPPPI PGFDKSGCLT DETIFDLPRL PEHLIIIGAG
ARGLEFAQAF RRLGSQVSVI DDANALGAED PEMTAVILRQ LREEGIDIRE HTRITHLTRL
GRHGVRVSFT TGHRALEGSH LLLATGRAPD LDGLDLGRAG IVHGEWGLKL DTRLRTTNHR
VYAIGDAAGA GESTAAARTH GELVVRAILF RLPLRVRPSM VPRIIFTDPE LAHVGLTETE
AAAKHRRLRV LRWPYAESDR AHIERSTHGH IKVVADSGGR ILGASIAGPM AGEMIHIWSL
ALAKGLTLRD MASYIAPYPS LGEIGKHAAI TYLIAAARMP FARRLIGILR KFG
//
