ID   MALZ_ECOLI              Reviewed;         605 AA.
AC   P21517; Q2MC23;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 4.
DT   03-NOV-2009, entry version 83.
DE   RecName: Full=Maltodextrin glucosidase;
DE            EC=3.2.1.20;
DE   AltName: Full=Alpha-glucosidase;
GN   Name=malZ; OrderedLocusNames=b0403, JW0393;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=92011742; PubMed=1918057;
RA   Tapio S., Yeh F., Shuman H.A., Boos W.;
RT   "The malZ gene of Escherichia coli, a member of the maltose regulon,
RT   encodes a maltodextrin glucosidase.";
RL   J. Biol. Chem. 266:19450-19458(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-605.
RC   STRAIN=K12;
RX   MEDLINE=91177815; PubMed=1706703;
RA   Reuter K., Slany R., Ullrich F., Kersten H.;
RT   "Structure and organization of Escherichia coli genes involved in
RT   biosynthesis of the deazaguanine derivative queuine, a nutrient factor
RT   for eukaryotes.";
RL   J. Bacteriol. 173:2256-2264(1991).
CC   -!- FUNCTION: May play a role in regulating the intracellular level of
CC       maltotriose. Cleaves glucose from the reducing end of maltotriose
CC       and longer maltodextrins with a chain length of up to 7 glucose
CC       units.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing (1->4)-
CC       linked alpha-D-glucose residues with release of alpha-D-glucose.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Under positive control of malT.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
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DR   EMBL; X59839; CAA42498.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U82664; AAB40159.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73506.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76183.1; -; Genomic_DNA.
DR   EMBL; M37702; AAA16112.1; -; Genomic_DNA.
DR   PIR; C64769; C64769.
DR   RefSeq; AP_001053.1; -.
DR   RefSeq; NP_414937.1; -.
DR   HSSP; Q59226; 1EA9.
DR   DIP; DIP:10152N; -.
DR   STRING; P21517; -.
DR   CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 949131; -.
DR   GenomeReviews; AP009048_GR; JW0393.
DR   GenomeReviews; U00096_GR; b0403.
DR   KEGG; ecj:JW0393; -.
DR   KEGG; eco:b0403; -.
DR   EchoBASE; EB0560; -.
DR   EcoGene; EG10565; malZ.
DR   HOGENOM; P21517; -.
DR   OMA; LKAPWSM; -.
DR   BioCyc; EcoCyc:MALTODEXGLUCOSID-MON; -.
DR   BioCyc; MetaCyc:MALTODEXGLUCOSID-MON; -.
DR   Genevestigator; P21517; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004558; F:alpha-glucosidase activity; IEA:EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006047; Glyco_hydro_13_cat.
DR   InterPro; IPR004185; Glyco_hydro_13_lg-like.
DR   InterPro; IPR006589; Glyco_hydro_13_sub_cat.
DR   InterPro; IPR013781; Glyco_hydro_sg_catalytic.
DR   InterPro; IPR017069; Maltodextrin_glucosidase.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02903; Alpha-amylase_N; 1.
DR   PIRSF; PIRSF036918; Maltodextrin_glucosidase; 1.
DR   SMART; SM00642; Aamy; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Glycosidase; Hydrolase;
KW   Maltose metabolism.
FT   CHAIN         1    605       Maltodextrin glucosidase.
FT                                /FTId=PRO_0000054334.
FT   ACT_SITE    337    337       Nucleophile (By similarity).
FT   ACT_SITE    374    374       Proton donor (By similarity).
FT   ACT_SITE    449    449       By similarity.
FT   CONFLICT    302    302       L -> M (in Ref. 1; CAA42498).
FT   CONFLICT    446    446       D -> E (in Ref. 1; CAA42498).
FT   CONFLICT    547    547       R -> S (in Ref. 1; CAA42498).
SQ   SEQUENCE   605 AA;  69172 MW;  80C200FDE11453EB CRC64;
     MMLNAWHLPV PPFVKQSKDQ LLITLWLTGE DPPQRIMLRT EHDNEEMSVP MHKQRSQPQP
     GVTAWRAAID LSSGQPRRRY SFKLLWHDRQ RWFTPQGFSR MPPARLEQFA VDVPDIGPQW
     AADQIFYQIF PDRFARSLPR EAEQDHVYYH HAAGQEIILR DWDEPVTAQA GGSTFYGGDL
     DGISEKLPYL KKLGVTALYL NPVFKAPSVH KYDTEDYRHV DPQFGGDGAL LRLRHNTQQL
     GMRLVLDGVF NHSGDSHAWF DRHNRGTGGA CHNPESPWRD WYSFSDDGTA LDWLGYASLP
     KLDYQSESLV NEIYRGEDSI VRHWLKAPWN MDGWRLDVVH MLGEAGGARN NMQHVAGITE
     AAKETQPEAY IVGEHFGDAR QWLQADVEDA AMNYRGFTFP LWGFLANTDI SYDPQQIDAQ
     TCMAWMDNYR AGLSHQQQLR MFNQLDSHDT ARFKTLLGRD IARLPLAVVW LFTWPGVPCI
     YYGDEVGLDG KNDPFCRKPF PWQVEKQDTA LFALYQRMIA LRKKSQALRH GGCQVLYAED
     NVVVFVRVLN QQRVLVAINR GEACEVVLPA SPFLNAVQWQ CKEGHGQLTD GILALPAISA
     TVWMN
//