ID K9T3W6_9CYAN Unreviewed; 482 AA.
AC K9T3W6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component {ECO:0000313|EMBL:AFY77592.1};
GN ORFNames=Ple7327_2283 {ECO:0000313|EMBL:AFY77592.1};
OS Pleurocapsa sp. PCC 7327.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Pleurocapsa.
OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY77592.1, ECO:0000313|Proteomes:UP000010382};
RN [1] {ECO:0000313|EMBL:AFY77592.1, ECO:0000313|Proteomes:UP000010382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY77592.1,
RC ECO:0000313|Proteomes:UP000010382};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished genome of Pleurocapsa sp. PCC 7327.";
RL Submitted (MAY-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}.
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DR EMBL; CP003590; AFY77592.1; -; Genomic_DNA.
DR RefSeq; WP_015143895.1; NC_019689.1.
DR AlphaFoldDB; K9T3W6; -.
DR STRING; 118163.Ple7327_2283; -.
DR KEGG; plp:Ple7327_2283; -.
DR PATRIC; fig|118163.3.peg.2544; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_3; -.
DR Proteomes; UP000010382; Chromosome.
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 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 Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Pyruvate {ECO:0000313|EMBL:AFY77592.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010382}.
FT DOMAIN 5..323
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 343..451
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 116
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"
SQ SEQUENCE 482 AA; 53031 MW; 40E7EA885D6DC488 CRC64;
MSVEYDLVVI GGSPEGIFAA IAAASLNARV ALVEQPFKVC WGDCETIYHS TFSHIAHLSR
QLDMAVQIGV YQPTPNLGIQ LTQVASWARE VNAILSERHA PAVLASLGID LIRGSGEFCR
LPRQAFVVGH KKLRSRKYLI ATDSHFVIPD ILGIEAVGYL TPNDLWQEDR LESLPGNLSI
IGESPVAIQL AQNFSQTGRS VTLIVADRHL LCAEDLEAAR LIQAQLEASG VEILLESPVT
QVLRIDGKKW LQAGDRAIEA DEIILVGKRK ANIDGLNLEG VGVRFDDRGI QLNEKLQTTN
PRIYACGSVA GGYSLSHVAR YEASIALKNA LFLPLLKVDY RAIPYVMFTN PPLARVGMTE
AQAKRRYGKD VWVVKQDFKA SDRAQLLGET TGFCKLVIRE NGEILGAHVV GPQAGELIGA
IALAMKNKIK LSSIASTSFP WLTFSEIVQK LALEWQNQRF KTNKTLQNFL ENLFTCLRDF
SS
//
