ID A0A0R1VSK1_9LACO Unreviewed; 441 AA.
AC A0A0R1VSK1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:KRM08714.1};
GN ORFNames=FC15_GL000321 {ECO:0000313|EMBL:KRM08714.1};
OS Lapidilactobacillus concavus DSM 17758.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lapidilactobacillus.
OX NCBI_TaxID=1423735 {ECO:0000313|EMBL:KRM08714.1, ECO:0000313|Proteomes:UP000051315};
RN [1] {ECO:0000313|EMBL:KRM08714.1, ECO:0000313|Proteomes:UP000051315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17758 {ECO:0000313|EMBL:KRM08714.1,
RC ECO:0000313|Proteomes:UP000051315};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM08714.1}.
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DR EMBL; AZFX01000078; KRM08714.1; -; Genomic_DNA.
DR RefSeq; WP_057825190.1; NZ_AZFX01000078.1.
DR AlphaFoldDB; A0A0R1VSK1; -.
DR STRING; 1423735.FC15_GL000321; -.
DR PATRIC; fig|1423735.3.peg.329; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000051315; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; 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; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
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 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051315}.
FT DOMAIN 2..310
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 333..434
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 441 AA; 48501 MW; 9C90311580D86E1F CRC64;
MFDVLFIGSG QGAWNGAIPM SQMGLKVAVV ESGQFGGVCT NRGCNAKITL DQPVELVQTI
RQLQGRGFDT VPTINWPDLM AHKQEVIGKL AESNKQKLID AGVTVIIGHA TLVDPTTVRV
NNQDYQAQKI VLALGQRPHE LTIPGAELTH DSTDFLAIPE MPQRLTIIGA GYVGMEFASI
ANAAGASVNV VVAGHRPLRG FYQPYVDRLV NSLRQRGVRF FFDQELTEVI SSTNGLTLKG
PHQFELTSDY ILNASGRVPN LENTGLEQLH IATNEHGIIV NDHLQTNIDT IYATGDVVAK
PQPKITPTAI FESQYLAQLF TGQTKAAIHY PSIATTVFSS PRISQVGISP DVAAKSPDQY
TIETFDYADD WFKQVQNEVD ASLTLVFDQA HLLVGAVEYS HEAVDSINGL LDVIEMRLTH
EQVQRFIYTF PSIQHSYFRK I
//
