ID U7PH76_SPOS1 Unreviewed; 568 AA.
AC U7PH76;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glutathione reductase {ECO:0000256|ARBA:ARBA00017111, ECO:0000256|RuleBase:RU365016};
DE EC=1.8.1.7 {ECO:0000256|ARBA:ARBA00012607, ECO:0000256|RuleBase:RU365016};
GN ORFNames=HMPREF1624_08619 {ECO:0000313|EMBL:ERS94908.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS94908.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
CC {ECO:0000256|ARBA:ARBA00003189, ECO:0000256|RuleBase:RU365016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7;
CC Evidence={ECO:0000256|RuleBase:RU365016};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365016}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; KI440857; ERS94908.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PH76; -.
DR STRING; 1391915.U7PH76; -.
DR eggNOG; KOG0405; Eukaryota.
DR HOGENOM; CLU_016755_2_2_1; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000018087; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; 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; IPR006322; Glutathione_Rdtase_euk/bac.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR NCBIfam; TIGR01421; gluta_reduc_1; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU365016};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW NADP {ECO:0000256|RuleBase:RU365016};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT DOMAIN 106..432
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 455..566
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 557
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 286..293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 376
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 417
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 143..148
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 568 AA; 60854 MW; 0799EF8DABB90D0D CRC64;
MSSASVCAAQ RFYKFASGTR ISTSTSTSTS AKQLFTTSRR PFASFSSTSP SPSTVVTTRM
RPFASLARAS TSRSLLPSSP SSRLASLSRQ LSSSARTMAP ISKETDYLVI GGGSGGLASA
RMASSKFGVK ATVIEGARLG GTCVNVGCVP KKVTFNAAAI AEALHEAKAY GFSVAETKPF
DWPTFKAKRD AYVKRLNGIY ERNLGNDKVE YVRGWARLTG RNEVTVALDE ADEAGHKEVT
IRAKKILVAV GGRPSDPPAI PGAEHGTNSD GFFEIATQPK KVAIVGAGYI AVEFAGMFNA
LGTETHLFIR GKTFLRTFDP LIQETVTDNY ANLGVHVHRE TQLTRVDKDA ATGKLTLTYG
DGQTLADVDH LIWAIGRTPL TKDIGLEEHG VELADKGFIK VDAFQNTTAE HIYALGDVTG
PVELTPVAIA AGRKLAHRLF GGPEFATLHQ DYTNIPSVVF AHPEVGSIGL TEPQAVDKFG
KDNVKVYKTN FTAMYYAMMD PDEKRPTAYK LVTTGKDEKV VGLHIAGLGS GEMLQGFGVA
IRMGATKKDF DNVVAIHPTS AEELVTLK
//
