ID L0ET67_LIBCB Unreviewed; 464 AA.
AC L0ET67;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 OrderedLocusNames=B488_07370 {ECO:0000313|EMBL:AGA64729.1};
OS Liberibacter crescens (strain BT-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA64729.1, ECO:0000313|Proteomes:UP000010799};
RN [1] {ECO:0000313|EMBL:AGA64729.1, ECO:0000313|Proteomes:UP000010799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-1 {ECO:0000313|EMBL:AGA64729.1,
RC ECO:0000313|Proteomes:UP000010799};
RX PubMed=23408754; DOI=10.4056/sigs.3326772;
RA Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., Triplett E.W.;
RT "Complete genome sequence of Liberibacter crescens BT-1.";
RL Stand. Genomic Sci. 7:271-283(2012).
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; CP003789; AGA64729.1; -; Genomic_DNA.
DR RefSeq; WP_015273156.1; NC_019907.1.
DR AlphaFoldDB; L0ET67; -.
DR STRING; 1215343.B488_07370; -.
DR KEGG; lcc:B488_07370; -.
DR PATRIC; fig|1215343.11.peg.759; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_2_1_5; -.
DR Proteomes; UP000010799; 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: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:UP000010799}.
FT DOMAIN 5..319
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 339..446
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 437
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 176..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 304
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 464 AA; 51225 MW; C723C9FC6B251A3E CRC64;
MSYDYDLFVI GAGSGGIRSA RLAAQLGKKV AIAEEYRLGG TCVIKGCIPK KILFYASQYS
EHLQDCLGFG WRVGQYDFDW KALISAKDNE ISRLENLYRD ILSRVGVDIL QARASLVDSH
TIHLENMNRA VTARHIVIAS GSSPNRMEAM PGHEFCITSD EIFFLEKLPE SILILGSGYI
AVEFANILHG FGVKTILLHR GKEVLSQFDS DIRQGLTRAM IDKGISIISE DHIKAIFQKG
MCLEAETKSG KSILVDQVLL ATGRKPNTGN MGLERAGVEI DSRNAICTNE YFQTNIQSIF
AIGDVINRVQ LTPVAIHEAM CFVETVFKNN PVFPDYDCIP TAVFSQPEVA CVGLTEEAAM
ATFPSLEIYK AQFKPMKSTL SMRSDYTIMK LIVNSVDRKV LGVHILGHVA SEMIQVIGVC
VKAGCSKDDF DRCIAVHPTA AEELVTIYSP SYYIKDGCKV SYQS
//
