ID A0A0K0XXU7_9GAMM Unreviewed; 453 AA.
AC A0A0K0XXU7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Glutathione reductase {ECO:0000256|RuleBase:RU365040};
DE Short=GRase {ECO:0000256|RuleBase:RU365040};
DE EC=1.8.1.7 {ECO:0000256|RuleBase:RU365040};
GN ORFNames=HNQ63_000161 {ECO:0000313|EMBL:MBB6085724.1}, WM2015_2136
GN {ECO:0000313|EMBL:AKS42500.1};
OS Wenzhouxiangella marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Wenzhouxiangellaceae; Wenzhouxiangella.
OX NCBI_TaxID=1579979 {ECO:0000313|EMBL:AKS42500.1, ECO:0000313|Proteomes:UP000066624};
RN [1] {ECO:0000313|EMBL:AKS42500.1, ECO:0000313|Proteomes:UP000066624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42284 {ECO:0000313|EMBL:AKS42500.1,
RC ECO:0000313|Proteomes:UP000066624};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6085724.1, ECO:0000313|Proteomes:UP000581413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103414 {ECO:0000313|EMBL:MBB6085724.1,
RC ECO:0000313|Proteomes:UP000581413};
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 (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Maintains high levels of reduced glutathione.
CC {ECO:0000256|RuleBase:RU365040}.
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|ARBA:ARBA00000669,
CC ECO:0000256|RuleBase:RU365040};
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 ECO:0000256|RuleBase:RU003691}.
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DR EMBL; CP012154; AKS42500.1; -; Genomic_DNA.
DR EMBL; JACHIC010000001; MBB6085724.1; -; Genomic_DNA.
DR RefSeq; WP_049726056.1; NZ_JACHIC010000001.1.
DR AlphaFoldDB; A0A0K0XXU7; -.
DR STRING; 1579979.WM2015_2136; -.
DR KEGG; wma:WM2015_2136; -.
DR PATRIC; fig|1579979.3.peg.2182; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000066624; Chromosome.
DR Proteomes; UP000581413; Unassembled WGS sequence.
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; IPR006324; GSHR.
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; TIGR01424; gluta_reduc_2; 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 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:RU365040};
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:UP000066624}.
FT DOMAIN 6..317
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 337..445
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 174..181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 453 AA; 48923 MW; 82EF79016813E911 CRC64;
MSQYDYDLFV IGAGSGGVRA SRIAAGHGAR VAICEESRVG GTCVIRGCVP KKLLVYASQF
AESFADASGY GWAVGESRFS WPDLIAAKDR EIDRLNGIYL RLLDSAGVEL HMGRGRIVDA
HTVAVGDRKF TAERILIAVG GRPFVPDIPG AELGITSDEA FHLEQLPERI LVVGAGYIAV
EFAGIFNGLG AQVTLAYRRD LVLRGFDRDI RQAVSDGMEG RGIDIHYHSE PAAIEQHGEA
LRVRFSDNDE REFDCVMFAT GREPYVADLG LESAGVRLGP GNRIEVDEFS RTNVDSIFAV
GDVTDRIALT PVALMEGHAF ADTEFGGMRR PVDHANVPAA VFSQPPVGCV GLSEEEARAA
GHRLRIFRSS FKPMKYTLAG REEQGVMKLV VDADSDRVLG VHVAGVDAPE ITQGFAVAVR
AGLTKADFDR TIGIHPTSAE ELVTLRQPIA EDQ
//
