ID S5QYH3_9STRE Unreviewed; 410 AA.
AC S5QYH3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:AGS06002.1};
GN ORFNames=KE3_1531 {ECO:0000313|EMBL:AGS06002.1};
OS Streptococcus lutetiensis 033.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS06002.1, ECO:0000313|Proteomes:UP000015268};
RN [1] {ECO:0000313|EMBL:AGS06002.1, ECO:0000313|Proteomes:UP000015268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=033 {ECO:0000313|EMBL:AGS06002.1,
RC ECO:0000313|Proteomes:UP000015268};
RX PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA Xu J.;
RT "Dynamics of fecal microbial communities in children with diarrhea of
RT unknown etiology and genomic analysis of associated Streptococcus
RT lutetiensis.";
RL BMC Microbiol. 13:141-141(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP003025; AGS06002.1; -; Genomic_DNA.
DR AlphaFoldDB; S5QYH3; -.
DR KEGG; slu:KE3_1531; -.
DR PATRIC; fig|1076934.5.peg.1494; -.
DR HOGENOM; CLU_016755_2_0_9; -.
DR Proteomes; UP000015268; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 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.
PE 4: Predicted;
FT DOMAIN 10..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..409
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 410 AA; 45024 MW; 5CE5F917682CF3EA CRC64;
MACGSDIVSG RKKVAIVEKD ITAGTCTNYG CSAKFLLDSP FEFIDSLSRY DKAGITGNTK
VNWQELMAYK KSEIPTYASL MEGMFAQMQI DLLKGYGKLV DAHTVSVDDD RISADYIVLG
TGQRPARLQI KGQKFLHDSC DFLDLDKMPK HITFIGAGII SMEFATMSAK LGSEVHIIEY
ADRALVAYQE NYIDSVVAKM TAEGVYFHFK QAVQAVEETT AGLRVTTAQG LELETDYVLD
VTGRIPNVEN LGPDELGIAY NRSGIVVNEY LQTSVPNIFA SGDVIDKNIP CLTSTASFES
DYIAAYILGV NQEAIQYPAI PNLVYTFPRI AQVGVSVVEG RENDAYRIVE IPFGQQLKFQ
TKLEDEAHVT LIVNQNKELV GASLLGNEAG EMINLLTLMI NQKVTANDLS
//
