ID L0DU11_THIND Unreviewed; 463 AA.
AC L0DU11;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:AGA32497.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:AGA32497.1};
GN Name=gor [H] {ECO:0000313|EMBL:AGA32497.1};
GN OrderedLocusNames=TVNIR_0807 {ECO:0000313|EMBL:AGA32497.1};
OS Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA32497.1, ECO:0000313|Proteomes:UP000010809};
RN [1] {ECO:0000313|Proteomes:UP000010809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC {ECO:0000313|Proteomes:UP000010809};
RA Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA Ravin N.V., Popov V.O.;
RT "Complete sequence of Thioalkalivibrio nitratireducens.";
RL Submitted (DEC-2012) 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; CP003989; AGA32497.1; -; Genomic_DNA.
DR RefSeq; WP_015257640.1; NC_019902.2.
DR AlphaFoldDB; L0DU11; -.
DR STRING; 1255043.TVNIR_0807; -.
DR KEGG; tni:TVNIR_0807; -.
DR PATRIC; fig|1255043.3.peg.813; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_2_2_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000010809; 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 4..316
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 338..447
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 438
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 172..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 41..46
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 463 AA; 49881 MW; 98B5F027C9120585 CRC64;
MEQYDIIVIG GGSGGLAVAE RAAGHGARVV VFDPKPLGGT CVNEGCVPKK LTWYAAHHIS
HARHASEFGV DLQSSGLRYP DLVQRRHAFL RMLNDYWSGY LERLGVDYVP ERAQLLDERT
VSAGGKEYRG ERVVIATGGE PIVPRMPGHE LGATSDDFFQ WEDLPRSIAI IGAGYIGLEM
AGMLRAFGAE VTVIAMEDRV LEMFDPMVSH VLERHLEEQG IERRLGATVK GLAGETGAVR
VQIADGSEAG PFERVLWAVG RSPRTRDIGL ESVGVELRPN GTVPVGEWQE TNVPGVFALG
DIIGKGPLTP VAIAAGRRLA DHWFAPERDP VPVDYSQIPT VTFTHPPTGA VGMTEPQAVA
RYGDQVHVYE TEFGGLARAF AEGDIAPISM KLVCAGDDER VVGIHMVGDA VDEMLQGFAV
AVRMGATKRD FDLTIPIHPT SAEELVTLKV SRPGQSDPVA NAA
//
