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Protein

Maltodextrin glucosidase

Gene

malZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May play a role in regulating the intracellular level of maltotriose. Cleaves glucose from the reducing end of maltotriose and longer maltodextrins with a chain length of up to 7 glucose units.

Catalytic activityi

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei336 – 3361NucleophileBy similarity
Active sitei373 – 3731Proton donorBy similarity
Sitei448 – 4481Transition state stabilizerBy similarity

GO - Molecular functioni

  • alpha-1,4-glucosidase activity Source: EcoCyc
  • cation binding Source: InterPro
  • maltose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  • alpha-glucan catabolic process Source: EcoCyc
  • cellular oligosaccharide catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Maltose metabolism

Enzyme and pathway databases

BioCyciEcoCyc:MALTODEXGLUCOSID-MONOMER.
ECOL316407:JW0393-MONOMER.
MetaCyc:MALTODEXGLUCOSID-MONOMER.
BRENDAi3.2.1.20. 2026.

Protein family/group databases

CAZyiCBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Maltodextrin glucosidase (EC:3.2.1.20)
Alternative name(s):
Alpha-glucosidase
Gene namesi
Name:malZ
Ordered Locus Names:b0403, JW0393
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10565. malZ.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 604604Maltodextrin glucosidasePRO_0000054334Add
BLAST

Expressioni

Inductioni

Under positive control of MalT.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-10152N.
IntActiP21517. 8 interactions.
MINTiMINT-1219352.
STRINGi511145.b0403.

Structurei

3D structure databases

ProteinModelPortaliP21517.
SMRiP21517. Positions 42-601.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000055363.
InParanoidiP21517.
KOiK01187.
OMAiDCRKCMI.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR014756. Ig_E-set.
IPR017069. MalZ.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036918. Maltodextrin_glucosidase. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

P21517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNAWHLPVP PFVKQSKDQL LITLWLTGED PPQRIMLRTE HDNEEMSVPM
60 70 80 90 100
HKQRSQPQPG VTAWRAAIDL SSGQPRRRYS FKLLWHDRQR WFTPQGFSRM
110 120 130 140 150
PPARLEQFAV DVPDIGPQWA ADQIFYQIFP DRFARSLPRE AEQDHVYYHH
160 170 180 190 200
AAGQEIILRD WDEPVTAQAG GSTFYGGDLD GISEKLPYLK KLGVTALYLN
210 220 230 240 250
PVFKAPSVHK YDTEDYRHVD PQFGGDGALL RLRHNTQQLG MRLVLDGVFN
260 270 280 290 300
HSGDSHAWFD RHNRGTGGAC HNPESPWRDW YSFSDDGTAL DWLGYASLPK
310 320 330 340 350
LDYQSESLVN EIYRGEDSIV RHWLKAPWNM DGWRLDVVHM LGEAGGARNN
360 370 380 390 400
MQHVAGITEA AKETQPEAYI VGEHFGDARQ WLQADVEDAA MNYRGFTFPL
410 420 430 440 450
WGFLANTDIS YDPQQIDAQT CMAWMDNYRA GLSHQQQLRM FNQLDSHDTA
460 470 480 490 500
RFKTLLGRDI ARLPLAVVWL FTWPGVPCIY YGDEVGLDGK NDPFCRKPFP
510 520 530 540 550
WQVEKQDTAL FALYQRMIAL RKKSQALRHG GCQVLYAEDN VVVFVRVLNQ
560 570 580 590 600
QRVLVAINRG EACEVVLPAS PFLNAVQWQC KEGHGQLTDG ILALPAISAT

VWMN
Length:604
Mass (Da):69,041
Last modified:November 16, 2011 - v5
Checksum:iB5A14754D7A42CCB
GO

Sequence cautioni

The sequence AAB40159.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE76183.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3011L → M in CAA42498 (PubMed:1918057).Curated
Sequence conflicti445 – 4451D → E in CAA42498 (PubMed:1918057).Curated
Sequence conflicti546 – 5461R → S in CAA42498 (PubMed:1918057).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59839 Genomic DNA. Translation: CAA42498.1.
U82664 Genomic DNA. Translation: AAB40159.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73506.2.
AP009048 Genomic DNA. Translation: BAE76183.1. Different initiation.
M37702 Genomic DNA. Translation: AAA16112.1.
PIRiC64769.
RefSeqiNP_414937.2. NC_000913.3.
WP_001310597.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC73506; AAC73506; b0403.
BAE76183; BAE76183; BAE76183.
GeneIDi949131.
KEGGieco:b0403.
PATRICi32115955. VBIEscCol129921_0419.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59839 Genomic DNA. Translation: CAA42498.1.
U82664 Genomic DNA. Translation: AAB40159.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73506.2.
AP009048 Genomic DNA. Translation: BAE76183.1. Different initiation.
M37702 Genomic DNA. Translation: AAA16112.1.
PIRiC64769.
RefSeqiNP_414937.2. NC_000913.3.
WP_001310597.1. NZ_CP010445.1.

3D structure databases

ProteinModelPortaliP21517.
SMRiP21517. Positions 42-601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10152N.
IntActiP21517. 8 interactions.
MINTiMINT-1219352.
STRINGi511145.b0403.

Protein family/group databases

CAZyiCBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73506; AAC73506; b0403.
BAE76183; BAE76183; BAE76183.
GeneIDi949131.
KEGGieco:b0403.
PATRICi32115955. VBIEscCol129921_0419.

Organism-specific databases

EchoBASEiEB0560.
EcoGeneiEG10565. malZ.

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000055363.
InParanoidiP21517.
KOiK01187.
OMAiDCRKCMI.

Enzyme and pathway databases

BioCyciEcoCyc:MALTODEXGLUCOSID-MONOMER.
ECOL316407:JW0393-MONOMER.
MetaCyc:MALTODEXGLUCOSID-MONOMER.
BRENDAi3.2.1.20. 2026.

Miscellaneous databases

PROiP21517.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR014756. Ig_E-set.
IPR017069. MalZ.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036918. Maltodextrin_glucosidase. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase."
    Tapio S., Yeh F., Shuman H.A., Boos W.
    J. Biol. Chem. 266:19450-19458(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes."
    Reuter K., Slany R., Ullrich F., Kersten H.
    J. Bacteriol. 173:2256-2264(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-604.
    Strain: K12.

Entry informationi

Entry nameiMALZ_ECOLI
AccessioniPrimary (citable) accession number: P21517
Secondary accession number(s): Q2MC23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 16, 2011
Last modified: July 22, 2015
This is version 128 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.