ID A0A1A7NU02_9PAST Unreviewed; 450 AA.
AC A0A1A7NU02;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:OBW92484.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:OBW92484.1};
GN ORFNames=QS62_08830 {ECO:0000313|EMBL:OBW92484.1}, QV08_06775
GN {ECO:0000313|EMBL:OBX07686.1};
OS Gallibacterium salpingitidis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=505341 {ECO:0000313|EMBL:OBW92484.1, ECO:0000313|Proteomes:UP000092649};
RN [1] {ECO:0000313|Proteomes:UP000092603, ECO:0000313|Proteomes:UP000092649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19987/2 Salp {ECO:0000313|EMBL:OBX07686.1,
RC ECO:0000313|Proteomes:UP000092603}, and F150
RC {ECO:0000313|EMBL:OBW92484.1, ECO:0000313|Proteomes:UP000092649};
RA Kudirkiene E., Bojesen A.M.;
RT "Pan-genome of Gallibacterium spp.";
RL Submitted (NOV-2014) 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}.
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:OBW92484.1}.
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DR EMBL; JTJL01000048; OBW92484.1; -; Genomic_DNA.
DR EMBL; JTJT01000030; OBX07686.1; -; Genomic_DNA.
DR RefSeq; WP_066108979.1; NZ_JTJU01000043.1.
DR AlphaFoldDB; A0A1A7NU02; -.
DR STRING; 505341.QV08_06775; -.
DR PATRIC; fig|505341.3.peg.1771; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000092603; Unassembled WGS sequence.
DR Proteomes; UP000092649; 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; IPR006322; Glutathione_Rdtase_euk/bac.
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; TIGR01421; gluta_reduc_1; 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 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:UP000092649}.
FT DOMAIN 5..318
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 339..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 51
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 262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 303
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 450 AA; 49038 MW; E84F04D7E0A2083D CRC64;
MMREYDYIAI GGGSGGIASI NRAASYGKKC AIIEAKYLGG TCVNVGCVPK KVMWYGAQIA
EAINLYAPDY GFDVTVNRFD FAKLRESREA YIDRIHQSYE RVLGNNKVDV IRGFAKFVDA
NTVEVNGEQI RAKHILIATG GRPSHPNIEG AEYGIDSDGV FALTELPKRV AVVGAGYIAV
ELAGVLHNLG VETHLFVRKH APLRNFDPLI VETLVEIMNN EGATLHTQAV PQKVVKNADG
SLTLFLEDGR SQTVDCLVWA IGRVPMTDNL NLEAAGVKTN SKGFIEVDKY QNTNVKGIYA
VGDNTGAVEL TPVAVAAGRR LSERLFNNKP NEHLDYNLIP TVVFSHPPIG TVGLTEPQAI
EQYGAEQVKV YKSTFTSMYT AVTQHRQPCR MKLVCVGAEE KIVGLHGIGF GVDEMIQGFA
VAIKMGATKK DFDNTVAIHP TGSEEFVTMR
//
