ID A0A1E3GSD5_9GAMM Unreviewed; 451 AA.
AC A0A1E3GSD5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 Name=gor {ECO:0000313|EMBL:ODN66937.1};
GN ORFNames=A9E74_01331 {ECO:0000313|EMBL:ODN66937.1};
OS Methylophaga muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=291169 {ECO:0000313|EMBL:ODN66937.1, ECO:0000313|Proteomes:UP000094379};
RN [1] {ECO:0000313|EMBL:ODN66937.1, ECO:0000313|Proteomes:UP000094379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bur 1 {ECO:0000313|EMBL:ODN66937.1,
RC ECO:0000313|Proteomes:UP000094379};
RA Vasilenko O.V., Doronina N.V., Shmareva M.N., Tarlachkov S.V.,
RA Mustakhimov I., Trotsenko Y.A.;
RT "Draft Genome Sequence of Methylophaga muralis Bur 1.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN66937.1}.
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DR EMBL; MCRI01000011; ODN66937.1; -; Genomic_DNA.
DR RefSeq; WP_069295813.1; NZ_MCRI01000011.1.
DR AlphaFoldDB; A0A1E3GSD5; -.
DR STRING; 291169.A9E74_01331; -.
DR PATRIC; fig|291169.3.peg.1337; -.
DR Proteomes; UP000094379; 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:UP000094379}.
FT DOMAIN 5..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 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 173..180
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 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 451 AA; 48585 MW; 530EB6BF089C4662 CRC64;
MKYDYDLFVI GAGSGGVRAS RMAASYGAKV AVCEDRYLGG TCVNVGCVPK KLYVYASEYS
SHFKDAKGFG WQVSKPTFDW STLRDNKTDE ISRLNGVYEG ILDRAGVEII DGRGKIVDAN
TVEVNGKTFT TERMLIATGG WPFIPDIPGK THAVDSNGIF DLAEFPQRLA VVGGGYIAVE
FAGIFHGLGS QVTQLVRGGG LLNGFDKEIA EFAAEQIQQN GVHIRFNTEV KSIKKQQDGS
LYLTMTDGQH LTVDAVLFAT GRKPHLDGLG LENVDIKLSK SGHIAVNKTF QTSEPSIYAL
GDVTGGIELT PVALAEGMAL AGYLFDKQPC KVDYSNIATT VFCQPNIGTV GMTEEQAREQ
YPNVLKFRSN FRAMKNTLGG SQQRTLMKLL VDADTDKVLG AHMVGESAGE IMQGIAIAMK
CGASKGDFDA TIGIHPTAAE EFVTMRTPVS D
//
