ID   MALZ_ECOLI              Reviewed;         604 AA.
AC   P21517; Q2MC23;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 5.
DT   25-JAN-2012, entry version 104.
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 191-604.
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40159.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAE76183.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; X59839; CAA42498.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40159.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73506.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76183.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M37702; AAA16112.1; -; Genomic_DNA.
DR   PIR; C64769; C64769.
DR   RefSeq; NP_414937.2; NC_000913.2.
DR   ProteinModelPortal; P21517; -.
DR   DIP; DIP-10152N; -.
DR   IntAct; P21517; 8.
DR   MINT; MINT-1219352; -.
DR   CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; EBESCT00000001930; EBESCP00000001930; EBESCG00000001583.
DR   EnsemblBacteria; EBESCT00000017691; EBESCP00000016982; EBESCG00000016747.
DR   GeneID; 949131; -.
DR   GenomeReviews; AP009048_GR; JW0393.
DR   GenomeReviews; U00096_GR; b0403.
DR   KEGG; ecj:JW0393; -.
DR   KEGG; eco:b0403; -.
DR   PATRIC; 32115955; VBIEscCol129921_0419.
DR   EchoBASE; EB0560; -.
DR   EcoGene; EG10565; malZ.
DR   eggNOG; COG0366; -.
DR   GeneTree; EBGT00050000009459; -.
DR   HOGENOM; HBG726713; -.
DR   OMA; HDNEETS; -.
DR   PhylomeDB; P21517; -.
DR   ProtClustDB; PRK10785; -.
DR   BioCyc; EcoCyc:MALTODEXGLUCOSID-MONOMER; -.
DR   BioCyc; MetaCyc:MALTODEXGLUCOSID-MONOMER; -.
DR   Genevestigator; P21517; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:EC.
DR   GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR015902; Alpha_amylase.
DR   InterPro; IPR013780; Glyco_hydro_13_b.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR   InterPro; IPR006589; Glyco_hydro_13_sub_cat_dom.
DR   InterPro; IPR013781; Glyco_hydro_subgr_catalytic.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR017069; Maltodextrin_glucosidase.
DR   Gene3D; G3DSA:2.60.40.1180; Glyco_hydro_13_b; 1.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   KO; K01187; -.
DR   PANTHER; PTHR10357; Alpha_amylase; 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.
DR   SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Glycosidase; Hydrolase;
KW   Maltose metabolism; Reference proteome.
FT   CHAIN         1    604       Maltodextrin glucosidase.
FT                                /FTId=PRO_0000054334.
FT   ACT_SITE    336    336       Nucleophile (By similarity).
FT   ACT_SITE    373    373       Proton donor (By similarity).
FT   SITE        448    448       Transition state stabilizer (By
FT                                similarity).
FT   CONFLICT    301    301       L -> M (in Ref. 1; CAA42498).
FT   CONFLICT    445    445       D -> E (in Ref. 1; CAA42498).
FT   CONFLICT    546    546       R -> S (in Ref. 1; CAA42498).
SQ   SEQUENCE   604 AA;  69041 MW;  B5A14754D7A42CCB CRC64;
     MLNAWHLPVP PFVKQSKDQL LITLWLTGED PPQRIMLRTE HDNEEMSVPM HKQRSQPQPG
     VTAWRAAIDL SSGQPRRRYS FKLLWHDRQR WFTPQGFSRM PPARLEQFAV DVPDIGPQWA
     ADQIFYQIFP DRFARSLPRE AEQDHVYYHH AAGQEIILRD WDEPVTAQAG GSTFYGGDLD
     GISEKLPYLK KLGVTALYLN PVFKAPSVHK YDTEDYRHVD PQFGGDGALL RLRHNTQQLG
     MRLVLDGVFN HSGDSHAWFD RHNRGTGGAC HNPESPWRDW YSFSDDGTAL DWLGYASLPK
     LDYQSESLVN EIYRGEDSIV RHWLKAPWNM DGWRLDVVHM LGEAGGARNN MQHVAGITEA
     AKETQPEAYI VGEHFGDARQ WLQADVEDAA MNYRGFTFPL WGFLANTDIS YDPQQIDAQT
     CMAWMDNYRA GLSHQQQLRM FNQLDSHDTA RFKTLLGRDI ARLPLAVVWL FTWPGVPCIY
     YGDEVGLDGK NDPFCRKPFP WQVEKQDTAL FALYQRMIAL RKKSQALRHG GCQVLYAEDN
     VVVFVRVLNQ QRVLVAINRG EACEVVLPAS PFLNAVQWQC KEGHGQLTDG ILALPAISAT
     VWMN
//