ID A0A1S8CIA4_9GAMM Unreviewed; 450 AA.
AC A0A1S8CIA4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:OMQ21004.1};
GN ORFNames=BMI79_15635 {ECO:0000313|EMBL:OMQ21004.1};
OS Serratia oryzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=2034155 {ECO:0000313|EMBL:OMQ21004.1, ECO:0000313|Proteomes:UP000216021};
RN [1] {ECO:0000313|EMBL:OMQ21004.1, ECO:0000313|Proteomes:UP000216021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J11-6 {ECO:0000313|EMBL:OMQ21004.1,
RC ECO:0000313|Proteomes:UP000216021};
RA Zhang X.-X., Zhang J.;
RT "Rahnella oryzae sp. nov., isolated from rice root.";
RL Submitted (NOV-2016) 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:OMQ21004.1}.
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DR EMBL; MOXD01000009; OMQ21004.1; -; Genomic_DNA.
DR RefSeq; WP_076943141.1; NZ_SOZF01000006.1.
DR AlphaFoldDB; A0A1S8CIA4; -.
DR STRING; 2034155.BMI79_15635; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000216021; 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:InterPro.
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}.
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; 48611 MW; 848965187BEC818D CRC64;
MTKHYDYLAI GGGSGGIASI NRAAMYGQKC ALIEAKELGG TCVNVGCVPK KVMWHAAQIA
EAIHQYGPDY GFDTTVNAFD WKKLVANRTA YIDRIHTSYD NVLGKNKVDV IKGFARFVDA
HTVEVNGETI TADHILIATG GRPSHPNIPG AEYGIDSDGF FELDAMPKRV AVVGAGYIAV
EIAGVMNALG AETHLFVRKH APLRSFDPMI VETLVEVMNT EGPQLHTESI PKAIVKNADG
SLTLQLENGK EFIVDCLVWA IGREPATDNL NLAVTGVKTN AKGYIEVDKF QNTSVKGVYA
VGDNTGAVEL TPVAVAAGRR LSERLFNNKP DEHLDYSNIA TVVFSHPPIG TIGLTEPQAK
EQFGEDNVKV YKSAFTAMYS AVTQHRQPCR MKLVCVGAEE KIVGLHGIGF GMDEILQGFA
VAVKMGATKK DFDNTVAIHP TAAEEFVTMR
//
