MALZ_ECOLI
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 03-AUG-2022, entry version 161.
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; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1918057; DOI=10.1016/s0021-9258(18)55017-1;
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 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-604.
RC STRAIN=K12;
RX PubMed=1706703; DOI=10.1128/jb.173.7.2256-2264.1991;
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 for
RT 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 and
CC longer maltodextrins with a chain length of up to 7 glucose units.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Under positive control of MalT.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE76183.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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_000913.3.
DR PDB; 5BN7; X-ray; 3.70 A; A=1-604.
DR PDBsum; 5BN7; -.
DR AlphaFoldDB; P21517; -.
DR SMR; P21517; -.
DR BioGRID; 4263268; 9.
DR DIP; DIP-10152N; -.
DR IntAct; P21517; 8.
DR MINT; P21517; -.
DR STRING; 511145.b0403; -.
DR CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR jPOST; P21517; -.
DR PaxDb; P21517; -.
DR PRIDE; P21517; -.
DR EnsemblBacteria; AAC73506; AAC73506; b0403.
DR EnsemblBacteria; BAE76183; BAE76183; BAE76183.
DR GeneID; 949131; -.
DR KEGG; ecj:JW0393; -.
DR KEGG; eco:b0403; -.
DR PATRIC; fig|511145.12.peg.419; -.
DR EchoBASE; EB0560; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_6_4_6; -.
DR InParanoid; P21517; -.
DR OMA; TPDWVKH; -.
DR PhylomeDB; P21517; -.
DR BioCyc; EcoCyc:MALTODEXGLUCOSID-MON; -.
DR BioCyc; MetaCyc:MALTODEXGLUCOSID-MON; -.
DR BRENDA; 3.2.1.20; 2026.
DR PRO; PR:P21517; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:EcoCyc.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030980; P:alpha-glucan catabolic process; IDA:EcoCyc.
DR GO; GO:0051692; P:cellular oligosaccharide catabolic process; IMP:EcoCyc.
DR CDD; cd02857; E_set_CDase_PDE_N; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR017069; MalZ.
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; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosidase; Hydrolase; Maltose metabolism;
KW Reference proteome.
FT CHAIN 1..604
FT /note="Maltodextrin glucosidase"
FT /id="PRO_0000054334"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 448
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 301
FT /note="L -> M (in Ref. 1; CAA42498)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="D -> E (in Ref. 1; CAA42498)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="R -> S (in Ref. 1; CAA42498)"
FT /evidence="ECO:0000305"
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
