ID A0A0A7EBF2_9GAMM Unreviewed; 451 AA.
AC A0A0A7EBF2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:AIY63823.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:AIY63823.1};
GN ORFNames=OM33_00555 {ECO:0000313|EMBL:AIY63823.1};
OS Pseudoalteromonas piratica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY63823.1, ECO:0000313|Proteomes:UP000030341};
RN [1] {ECO:0000313|EMBL:AIY63823.1, ECO:0000313|Proteomes:UP000030341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY63823.1,
RC ECO:0000313|Proteomes:UP000030341};
RA Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA Belcaid M.;
RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT from Kaneohe Bay, Oahu, Hawaii.";
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}.
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DR EMBL; CP009888; AIY63823.1; -; Genomic_DNA.
DR RefSeq; WP_038637380.1; NZ_CP009888.1.
DR AlphaFoldDB; A0A0A7EBF2; -.
DR STRING; 1348114.OM33_00555; -.
DR KEGG; pseo:OM33_00555; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_2_2_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000030341; Chromosome 1.
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:UP000030341}.
FT DOMAIN 6..319
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 341..451
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 441
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 451 AA; 48538 MW; 861DAC9F00D9785B CRC64;
MAKHFDYIAI GGGSGGIASA NRAAMRGANV ALVEAGPLGG TCVNVGCVPK KVMWHGAQVA
EAIKLYAPDY GFDVKIKEFN WAKLLESREA YIGRIHNGYD NYLAKNGVTV IQGFAKFVDN
KTIEVNGEHY TADHILVAVG GRPSIPNIPG AEYGIDSNGF FELKEQPKRV AVVGAGYIAV
ELAGVMHGLG TETHLCVRRD TPLRTFDPLI VDTLMEVIES EGPTLHTNAT PKEVTKESDG
SLTLHFENGN SVNVDQVIWA IGRQPTTDKI NIAAAGVELT ESGHVKVDEF QNTTAEGVYA
VGDIIENGIE LTPVAVKAGR LLSERLFNPE MPNAKMDYNL VPTVVFSHPP IGTIGLTETD
AREQFGDDDI KVYTSSFTAM YTAVTQHRQP CKMKLVCQGP NEKIVGLHGI GFAVDEMIQG
FGVAMKMGAT KADFDSVVAI HPTGSEEFVT M
//
