ID A0A090U208_9VIBR Unreviewed; 62 AA.
AC A0A090U208;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:GAL37032.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:GAL37032.1};
GN ORFNames=JCM19240_2981 {ECO:0000313|EMBL:GAL37032.1};
OS Vibrio maritimus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=990268 {ECO:0000313|EMBL:GAL37032.1, ECO:0000313|Proteomes:UP000029224};
RN [1] {ECO:0000313|EMBL:GAL37032.1, ECO:0000313|Proteomes:UP000029224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL37032.1,
RC ECO:0000313|Proteomes:UP000029224};
RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RT "Vibrio maritimus JCM 19240. (C210) whole genome shotgun sequence.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAL37032.1, ECO:0000313|Proteomes:UP000029224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL37032.1,
RC ECO:0000313|Proteomes:UP000029224};
RG NBRP consortium;
RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:GAL37032.1}.
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DR EMBL; BBMT01000014; GAL37032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090U208; -.
DR Proteomes; UP000029224; 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:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR046952; GSHR/TRXR-like.
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 PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:GAL37032.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000029224}.
FT DOMAIN 5..61
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 62 AA; 6282 MW; 13D20A69D6433BA9 CRC64;
MATHFDYICI GGGSGGIASA NRAAMYGAKV ALIEAKDLGG TCVNVGCVPK KVMWHGAQIA
EA
//