GenomeNet

Database: UniProt
Entry: I0IBW6_PHYMF
LinkDB: I0IBW6_PHYMF
Original site: I0IBW6_PHYMF 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system