ID A0A0R2AWC3_9LACO Unreviewed; 449 AA.
AC A0A0R2AWC3;
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:KRM67539.1};
GN ORFNames=FD06_GL000690 {ECO:0000313|EMBL:KRM67539.1};
OS Apilactobacillus ozensis DSM 23829 = JCM 17196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Apilactobacillus.
OX NCBI_TaxID=1423781 {ECO:0000313|EMBL:KRM67539.1, ECO:0000313|Proteomes:UP000052012};
RN [1] {ECO:0000313|EMBL:KRM67539.1, ECO:0000313|Proteomes:UP000052012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23829 {ECO:0000313|EMBL:KRM67539.1,
RC ECO:0000313|Proteomes:UP000052012};
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:KRM67539.1}.
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DR EMBL; AYYQ01000036; KRM67539.1; -; Genomic_DNA.
DR RefSeq; WP_056967000.1; NZ_AYYQ01000036.1.
DR AlphaFoldDB; A0A0R2AWC3; -.
DR STRING; 1423781.FD06_GL000690; -.
DR PATRIC; fig|1423781.4.peg.708; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000052012; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000052012}.
FT DOMAIN 5..315
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 339..427
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 449 AA; 49778 MW; 6035684691FAAC7D CRC64;
MNKKYDVMFL GSGHANWHGA LKLAKNGKKV ALIEGDKIFG TCTNYGCNAK FLLDRPADII
NQVDSDNALK GKVQIDWKVL MNHKHKMLDS NPDHQEVRKS FPKLGVDIIN GWGTIKDAHH
IEVENDTYET DYIVIGTGLR ASKLNIDGKE YLKESRDFLS IPDMPKHITI IGTGVIAYEF
ADLANAAGAK VEVIGHSDKP LRNFDSEFVN KLTSRMKNRG IEFHFNQNIE SVSKSDNGFI
LKTKEKLNIN TEYVLDATGR VANYEKLGLD KLGIEASPKG IKVNNHLRTS VYNIFVSGDA
IDKKQPKLTP TATYESNYIA KDILSNHNPS IKYPPIVEAL FSLPRLAQVG VKPNDVKDNN
DYTIKSFKYG LLVFEPLNDN TSEAKIVLNS ENQIVGATIL GSQSVQIANA LSIIISNKMT
PEEVNDSAIM AFPDEIYGLV QLLTGEIPG
//
