ID I0IBW6_PHYMF Unreviewed; 465 AA.
AC I0IBW6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative glutathione reductase {ECO:0000313|EMBL:BAM02754.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:BAM02754.1};
GN OrderedLocusNames=PSMK_05950 {ECO:0000313|EMBL:BAM02754.1};
OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM02754.1, ECO:0000313|Proteomes:UP000007881};
RN [1] {ECO:0000313|EMBL:BAM02754.1, ECO:0000313|Proteomes:UP000007881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC {ECO:0000313|Proteomes:UP000007881};
RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AP012338; BAM02754.1; -; Genomic_DNA.
DR RefSeq; WP_014435974.1; NC_017080.1.
DR AlphaFoldDB; I0IBW6; -.
DR STRING; 1142394.PSMK_05950; -.
DR GeneID; 80849403; -.
DR KEGG; phm:PSMK_05950; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_2_0_0; -.
DR OrthoDB; 230580at2; -.
DR Proteomes; UP000007881; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
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; 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;
KW Oxidoreductase {ECO:0000313|EMBL:BAM02754.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007881}.
FT DOMAIN 8..326
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"
SQ SEQUENCE 465 AA; 47651 MW; CF28C723DA0C3F07 CRC64;
MSRTHAFDRV VLGSGAVGQT AAYNGRERGC SVLLVEAGDF GGTCPNRGCD AKKPYVHAAA
VVHAVQRLQA AGGGVVGELS MDWSRTAAFK KSFTRVTDPR TRQDLAAAGV ELHAGTAAFT
GPDTLRLSDG REVRAGAVVV ATGQHPRPLE IPGGALAIDS DAFLELDDLP PRVAMIGSGY
IGMEFACAAA LAGREVVVIG SREHPLTGFD ADAVAVLEAA LPTLGPHGVR LVAGARATRL
EPRGDGVAVF TDADAPAAVA DLVVNATGRV ASVDGLGLEA AGVEAGAAGV KVDATLRSPG
NPRVWAGGDV ADTGRPALIP TAVADARVLV KNLAAAANGG ALLEVEDQPI ATVAFTTPTL
ASVGLTEADA RRAHGGALHV ASGDLTTKKF YRQLGVEHAF YKLIFDADRR LIGAHLAGPE
SEEVVNVFAV AIHEGCSQSR LCDAVLTYPT VSAAMQAAYR KTARG
//