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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//