ID F9P5E9_STRCV Unreviewed; 449 AA.
AC F9P5E9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:EGV10874.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:EGV10874.1};
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component {ECO:0000313|EMBL:GAD43611.1};
GN Name=gor {ECO:0000313|EMBL:EGV10874.1};
GN ORFNames=ANG5_0139 {ECO:0000313|EMBL:GAD43611.1}, HMPREF1042_0703
GN {ECO:0000313|EMBL:EGV10874.1};
OS Streptococcus constellatus subsp. pharyngis SK1060 = CCUG 46377.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1035184 {ECO:0000313|EMBL:EGV10874.1, ECO:0000313|Proteomes:UP000003287};
RN [1] {ECO:0000313|EMBL:EGV10874.1, ECO:0000313|Proteomes:UP000003287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1060 {ECO:0000313|EMBL:EGV10874.1,
RC ECO:0000313|Proteomes:UP000003287};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAD43611.1, ECO:0000313|Proteomes:UP000016985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 46377 {ECO:0000313|EMBL:GAD43611.1}, and CCUG46377
RC {ECO:0000313|Proteomes:UP000016985};
RA Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y.,
RA Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., Hayashi T.,
RA Shintani S.;
RT "Genome Sequences of seven clinical isolates and type strains of anginosus
RT group streptococci.";
RL Submitted (SEP-2013) 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; AFUP01000001; EGV10874.1; -; Genomic_DNA.
DR EMBL; BASX01000001; GAD43611.1; -; Genomic_DNA.
DR RefSeq; WP_006267503.1; NZ_BASX01000001.1.
DR AlphaFoldDB; F9P5E9; -.
DR eggNOG; COG1249; Bacteria.
DR Proteomes; UP000003287; Unassembled WGS sequence.
DR Proteomes; UP000016985; 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}; Pyruvate {ECO:0000313|EMBL:GAD43611.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 4..317
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 338..448
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 173..180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 302
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 449 AA; 48921 MW; 5148FBFF8852D706 CRC64;
MRTFDIIAIG GGSGGIASMN RAGEHGAKAA VIEEKKLGGT CVNVGCVPKK IMWYGAQIAE
AIQDYGPDYG FTSDNQQFDF RTLRKNREAY IDRARHSYHN SFTRNGVEVI EGRAKFIDRH
TVEVNGEIIQ AKHIVIATGA HPHIPAIPGA ELGETSDDVF AWEELPQSVA ILGAGYIAVE
LAGLLHALGV KTDLFVRRER PLRNFDAYII EGLVEEMKKS GPTLHTHKIP KKLEKVENDL
LRITFEDGTS HFAQHVIWAT GRTANTKGVN LEAAGVTLDT RGFITVDEFQ NTATSGIYAL
GDVTGEKELT PVAIKAGRTL AERLFNGKSE AKMDYSNIPT VVFSHPAIGT VGLTEEQAIQ
QYGAENLHIY TSGFTSMYSA VTQHRQQAKF KLITTGTDEK VIGLHGIGYG VDEMIQGFAV
AIKMGATKAD FDATVAIHPT GSEEFVTMR
//
