ID A0A0R0DZ76_9GAMM Unreviewed; 450 AA.
AC A0A0R0DZ76;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:KRG83591.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:KRG83591.1};
GN Name=gor {ECO:0000313|EMBL:ALJ28758.1};
GN ORFNames=ABB33_13740 {ECO:0000313|EMBL:KRG83591.1}, AOT14_23920
GN {ECO:0000313|EMBL:ALJ28758.1};
OS Stenotrophomonas acidaminiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=128780 {ECO:0000313|EMBL:KRG83591.1, ECO:0000313|Proteomes:UP000050958};
RN [1] {ECO:0000313|EMBL:ALJ28758.1, ECO:0000313|Proteomes:UP000061010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZAC14D2_NAIMI4_2 {ECO:0000313|EMBL:ALJ28758.1,
RC ECO:0000313|Proteomes:UP000061010};
RX PubMed=26659678;
RA Vinuesa P., Ochoa-Sanchez L.E.;
RT "Complete Genome Sequencing of Stenotrophomonas acidaminiphila
RT ZAC14D2_NAIMI4_2, a Multidrug-Resistant Strain Isolated from Sediments of a
RT Polluted River in Mexico, Uncovers New Antibiotic Resistance Genes and a
RT Novel Class-II Lasso Peptide Biosynthesis Gene Cluster.";
RL Genome Announc. 3:e01433-15(2015).
RN [2] {ECO:0000313|EMBL:KRG83591.1, ECO:0000313|Proteomes:UP000050958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13310 {ECO:0000313|EMBL:KRG83591.1,
RC ECO:0000313|Proteomes:UP000050958};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012900; ALJ28758.1; -; Genomic_DNA.
DR EMBL; LDJO01000047; KRG83591.1; -; Genomic_DNA.
DR RefSeq; WP_054666674.1; NZ_LDJO01000047.1.
DR AlphaFoldDB; A0A0R0DZ76; -.
DR KEGG; sacz:AOT14_23920; -.
DR PATRIC; fig|128780.6.peg.2410; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000050958; Unassembled WGS sequence.
DR Proteomes; UP000061010; 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 GO; GO:0045454; P:cell redox homeostasis; 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; 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 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 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}.
FT DOMAIN 6..320
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 341..449
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 439
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 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 141..143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 176..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 305
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 450 AA; 47180 MW; B09EB9D94A614B2A CRC64;
MSPPSFDVIV LGGGSGGLAA AFRAASHGAK VAMLEPALLG GTCVNVGCVP KKAMWLAADL
AERITLAAGL GFEVPAAPRL SWPRLLQRRQ RYIDGIHASY RQRLQDSGVA HIAQRGRLLD
ARTVECGDGT LLHARHIVIA TGSHALKPQL PGAALGGTSD DFFALQAPPA RVAIVGGGYI
AVELAGVMQA LGSDVTLLVR GQRLLTGFDA GMTEQLARNL AAQGVAVRFG CQVQALQRRG
DGIQPHLQGG PADAVFDTVL FATGRAPSTH GLGLEAAGVA LDDKGAIVVD AFQDTSVQGI
SAVGDVTAQA MLTPVAIAAA RRLMDRLYGG QPEARLDYDN IPSVVFSHPP LGSVGLSEEQ
ARERFDSVST YHSRFRPMLQ ALGDGEMRSL FKMVCAGADE KVVGIHLLGE GADEILQGFA
VALKAGVTRR QMEDTVAIHP TSAEEVVLMR
//
