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Database: UniProt
Entry: A0A0R1MYY4_9LACO
LinkDB: A0A0R1MYY4_9LACO
Original site: A0A0R1MYY4_9LACO 
ID   A0A0R1MYY4_9LACO        Unreviewed;       280 AA.
AC   A0A0R1MYY4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=2,5-didehydrogluconate reductase {ECO:0000313|EMBL:KRL13311.1};
GN   ORFNames=FD09_GL002138 {ECO:0000313|EMBL:KRL13311.1};
OS   Schleiferilactobacillus perolens DSM 12744.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Schleiferilactobacillus.
OX   NCBI_TaxID=1423792 {ECO:0000313|EMBL:KRL13311.1, ECO:0000313|Proteomes:UP000051330};
RN   [1] {ECO:0000313|EMBL:KRL13311.1, ECO:0000313|Proteomes:UP000051330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12744 {ECO:0000313|EMBL:KRL13311.1,
RC   ECO:0000313|Proteomes:UP000051330};
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   -!- 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:KRL13311.1}.
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DR   EMBL; AZEC01000004; KRL13311.1; -; Genomic_DNA.
DR   RefSeq; WP_057819193.1; NZ_AZEC01000004.1.
DR   AlphaFoldDB; A0A0R1MYY4; -.
DR   STRING; 1423792.FD09_GL002138; -.
DR   PATRIC; fig|1423792.3.peg.2180; -.
DR   OrthoDB; 9804790at2; -.
DR   Proteomes; UP000051330; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd19133; AKR_AKR5F1; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43827; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 1.
DR   PANTHER; PTHR43827:SF3; ALDO_KET_RED DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 2.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   4: Predicted;
FT   DOMAIN          23..258
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        49
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            74
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   280 AA;  31649 MW;  8F9934F36BD2F01D CRC64;
     MDTVKLNNGV EMPIAGFGVF QIQDQDQAEQ AVVDAIHAGY RLIDTAQAYG NEEAVGKGIK
     RSGVPRDQLF ITTKVWITDV GYEKTQKAID TSLQKLGLDY LDLYLIHQPY NDVYGAWRAM
     QEAEQAGKIR AIGVSNFEPD RLMDLSAFSG VTPTVNQIEI NPWQQQKEAL AFMAKENIQP
     EAWAPFAEGK HDIFHNPLLE AIGKKYGKSV GQVILRWVVQ QHIVALAKSV HAERMAENID
     IFDFQLSDDD MAQISQLDRH ESQFFDHRDP EQIKRLATLH
//
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