ID J0UUV0_9LACO Unreviewed; 319 AA.
AC J0UUV0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=2,5-diketo-D-gluconic acid reductase {ECO:0000313|EMBL:KRN09952.1};
GN ORFNames=FD00_GL000579 {ECO:0000313|EMBL:KRN09952.1};
OS Liquorilactobacillus mali KCTC 3596 = DSM 20444.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1046596 {ECO:0000313|EMBL:KRN09952.1, ECO:0000313|Proteomes:UP000050898};
RN [1] {ECO:0000313|EMBL:KRN09952.1, ECO:0000313|Proteomes:UP000050898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20444 {ECO:0000313|EMBL:KRN09952.1,
RC ECO:0000313|Proteomes:UP000050898};
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:KRN09952.1}.
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DR EMBL; AYYH01000016; KRN09952.1; -; Genomic_DNA.
DR RefSeq; WP_003687237.1; NZ_BACP01000068.1.
DR AlphaFoldDB; J0UUV0; -.
DR PATRIC; fig|1046596.6.peg.620; -.
DR OrthoDB; 9804790at2; -.
DR Proteomes; UP000050898; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd19132; AKR_AKR5D1_E1; 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-KETO REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
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 58..302
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 116
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 319 AA; 36112 MW; 316451E821FE51F9 CRC64;
MSENVLFNQG QAISSKYDFS KTYLSAELFK KKNGSGPEPS ANQPELITLS DGNEIPLIGF
GTYTLTGGSG VNTMMQALST GYRALDSAVN YENEGAVGEV IRRSSLKRED LFITSKLPGR
HQKFDEAITT IQESLFRMHL DYFDLYLIHW PNPLENHYVE AWQALIEAQK MGLIRSIGVS
NFLPEHLERL EKETGVLPVV NQIELHPYWS QPEQRKFDKE HGIFTQAWSP LGRANAVLHD
EIIKKIAETH HKSIAQVILR WELQLGVGVI PKSSSTKRQF ENLDLFNFEL SDEEISSISA
LDKPDGRTNS QNPAVYQEF
//