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Database: UniProt
Entry: Q631Q4_BACCZ
LinkDB: Q631Q4_BACCZ
Original site: Q631Q4_BACCZ 
ID   Q631Q4_BACCZ            Unreviewed;       279 AA.
AC   Q631Q4;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Oxidoreductase, aldo/keto reductase family {ECO:0000313|EMBL:AAU15485.1};
GN   OrderedLocusNames=BCE33L4792 {ECO:0000313|EMBL:AAU15485.1};
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU15485.1, ECO:0000313|Proteomes:UP000002612};
RN   [1] {ECO:0000313|Proteomes:UP000002612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA   Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA   Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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DR   EMBL; CP000001; AAU15485.1; -; Genomic_DNA.
DR   RefSeq; WP_000793529.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q631Q4; -.
DR   KEGG; bcz:BCE33L4792; -.
DR   PATRIC; fig|288681.22.peg.562; -.
DR   Proteomes; UP000002612; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd19157; AKR_AKR5G1-3; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044500; AKR5G.
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:SF1; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 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          30..265
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        53
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            82
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   279 AA;  31707 MW;  97DEA30E7514369F CRC64;
     MKNLQSKAVL NNGVEMPWFG LGVFKVEEGP ELVEAVKAAI KAGYRSIDTA AIYGNEKAVG
     EGIRAGIEAT GIAREDLFIT SKVWNADQGY ETTIAAYEES LKKLGLDYLD LYLVHWPSEG
     KYKDTWRALE TLYKEKRVRA IGVSNFQIHH LQDVMKDAEI KPMINQVEYH PRLTQKELQA
     FCKEQGIQME AWSPLMQGQL LDNETLQEIA EKHGKTTAQV ILRWDLQNGV ITIPKSTKEH
     RIIANADVFN FELTKEDMEK IDALNQNHRV GPDPDNFDF
//
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