ID I1ZMZ9_STRPA Unreviewed; 449 AA.
AC I1ZMZ9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:AFJ26423.1};
GN ORFNames=Spaf_1452 {ECO:0000313|EMBL:AFJ26423.1};
OS Streptococcus parasanguinis FW213.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1114965 {ECO:0000313|EMBL:AFJ26423.1, ECO:0000313|Proteomes:UP000002865};
RN [1] {ECO:0000313|EMBL:AFJ26423.1, ECO:0000313|Proteomes:UP000002865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW213 {ECO:0000313|EMBL:AFJ26423.1,
RC ECO:0000313|Proteomes:UP000002865};
RX PubMed=22529932; DOI=10.1371/journal.pone.0034769;
RA Geng J., Chiu C.H., Tang P., Chen Y., Shieh H.R., Hu S., Chen Y.Y.;
RT "Complete Genome and Transcriptomes of Streptococcus parasanguinis FW213:
RT Phylogenic Relations and Potential Virulence Mechanisms.";
RL PLoS ONE 7:E34769-E34769(2012).
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; CP003122; AFJ26423.1; -; Genomic_DNA.
DR RefSeq; WP_014713634.1; NC_017905.1.
DR AlphaFoldDB; I1ZMZ9; -.
DR STRING; 1114965.Spaf_1452; -.
DR PaxDb; 1114965-Spaf_1452; -.
DR KEGG; scf:Spaf_1452; -.
DR PATRIC; fig|1114965.3.peg.1394; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_2_2_9; -.
DR Proteomes; UP000002865; Chromosome.
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..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; 49366 MW; B13CCDB0F351903F CRC64;
MKEFDIISIG GGSGGIATMN RAGEHGARAA VIEEKQLGGT CVNRGCVPKK IMWYGAQIAE
AIRDYGPDYG FTSEQTRFDF ATLRKNREAY IDRSRNSYDG SFKRNGVERI EGRARFVDAH
TIEVNGETIK AKHIVIATGA HPFIPSVPGA EFGETSDDVF AWEELPSSVA IIGAGYIAVE
LAGVLHHLGV QTDLFIRKDR VLRSFDSYIV DGLMEEMKKQ NLPLHKHKVP MKLEKLEDGR
VKIYFEDMTS HVADHVIWAT GRKPNVQDLN LEAAGVTLNE KGFIAVDEYQ NTVIPGIYAL
GDVTGEKELT PVAIKAGRTL SERLFNGKVN AKMDYTNIPT VVFSHPSIGT VGLTEEEAQQ
TYGKENIKVY TSQFASMYTA VTQHRQQAKF KLITAGPEEK VVGLHGLGYG VDEMIQGFAV
AIKMGATKAD FDATVAIHPT GSEEFVTMR
//
