ID Q03I10_PEDPA Unreviewed; 288 AA.
AC Q03I10;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Aldo/keto reductase of diketogulonate reductase family {ECO:0000313|EMBL:ABJ67162.1};
GN OrderedLocusNames=PEPE_0051 {ECO:0000313|EMBL:ABJ67162.1};
OS Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS 183-1w).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=278197 {ECO:0000313|EMBL:ABJ67162.1, ECO:0000313|Proteomes:UP000000773};
RN [1] {ECO:0000313|EMBL:ABJ67162.1, ECO:0000313|Proteomes:UP000000773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w
RC {ECO:0000313|Proteomes:UP000000773};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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DR EMBL; CP000422; ABJ67162.1; -; Genomic_DNA.
DR RefSeq; WP_011672795.1; NC_008525.1.
DR AlphaFoldDB; Q03I10; -.
DR STRING; 278197.PEPE_0051; -.
DR GeneID; 33062014; -.
DR KEGG; ppe:PEPE_0051; -.
DR eggNOG; COG0656; Bacteria.
DR HOGENOM; CLU_023205_0_1_9; -.
DR OrthoDB; 9804790at2; -.
DR Proteomes; UP000000773; Chromosome.
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; cd19071; AKR_AKR1-5-like; 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.
PE 4: Predicted;
FT DOMAIN 19..270
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 52
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 77
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 288 AA; 32299 MW; E32CB65017435DA1 CRC64;
MNVFEESYKL SNGVKIPKLA LGTWEIDDDQ VADAVRSAIE MGYRHIDTAQ AYANERGVGE
GVRTASVPRE EIFVNSKIAA EIKNYDDAKK SIDETLNKMG LDYLDMMIIH NPQPWAEVNQ
SDDRHFEGNL EVWRALEDAM HEGKLRAIGV SSFQKEDLDN LIKNSDTKPM VNQILSHIAA
TPMDLINYSH ENGIVVEAFS PIAHGQALRS EAIQKMAAKY NVSAPQLSIR YDWQLDTVVL
PKTSNPEHMK SNAELDFVIS DEDMEILKQV KPLDYGDASV FPVFGGKM
//
