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Database: UniProt
Entry: A0A0U3PNA8_9LACT
LinkDB: A0A0U3PNA8_9LACT
Original site: A0A0U3PNA8_9LACT 
ID   A0A0U3PNA8_9LACT        Unreviewed;       449 AA.
AC   A0A0U3PNA8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Glutathione reductase {ECO:0000313|EMBL:ALV21840.1};
GN   ORFNames=NY10_1231 {ECO:0000313|EMBL:ALV21840.1};
OS   Carnobacterium sp. CP1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV21840.1, ECO:0000313|Proteomes:UP000064734};
RN   [1] {ECO:0000313|EMBL:ALV21840.1, ECO:0000313|Proteomes:UP000064734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP1 {ECO:0000313|EMBL:ALV21840.1,
RC   ECO:0000313|Proteomes:UP000064734};
RA   Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT   "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT   Amanda bay, East Antarctic.";
RL   Submitted (FEB-2015) 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; CP010796; ALV21840.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U3PNA8; -.
DR   STRING; 1564681.NY10_1231; -.
DR   KEGG; carc:NY10_1231; -.
DR   PATRIC; fig|1564681.3.peg.1230; -.
DR   Proteomes; UP000064734; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064734}.
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;  48555 MW;  89EA1D777B51F26F CRC64;
     MKQYDYIAIG GGSGGIASIN RAGMHGAKGA LIEGNAIGGT CVNVGCVPKK IMWHGAQMMD
     EMNLYASGYG IDIPSKNLNF AKLVENRETF IERLHGSYQN GLASNEVDLI HGYAKFVDNK
     TVEVNGEQYT ADHILIATGG KPVFPDIPGA EYGLDSDGFF EMTELPKRTA VVGAGYIAVE
     LAGVLHGLGS DTHLFVRQHA PLRNFDSIIV EGLVETMERE GATLHTYAVP EKVEKNEDGS
     LTLYLKDGTA HETDAVIWAI GREPNTDSLN LAATDVAVND GGYIKVDEFQ NTSVKGIYAV
     GDVTGHIELT PVAIAAGRRL SERLFNNKPM EHLDYNNVPT VVFTHPPIGT VGMTEEQAVD
     VYGKAQIKTY ETRFTAMHSS ITENRQKTYM KLVCCGPEEK VVGLHGMGSG MDEMLQGFAV
     AIKMGATKAD FDDTVAIHPT GAEEFVTMR
//
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