Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P21517

- MALZ_ECOLI

UniProt

P21517 - MALZ_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Maltodextrin glucosidase

Gene

malZ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 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

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

GO - Biological processi

  1. alpha-glucan catabolic process Source: EcoCyc
  2. cellular oligosaccharide catabolic process Source: EcoCyc
  3. maltose metabolic process Source: UniProtKB-KW
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.

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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10565. malZ.

Subcellular locationi

GO - Cellular componenti

  1. 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.

Gene expression databases

GenevestigatoriP21517.

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.
OMAiGNNDPFC.

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.
YP_488695.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73506; AAC73506; b0403.
BAE76183; BAE76183; BAE76183.
GeneIDi12934274.
949131.
KEGGiecj:Y75_p0391.
eco: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 .
PIRi C64769.
RefSeqi NP_414937.2. NC_000913.3.
YP_488695.1. NC_007779.1.

3D structure databases

ProteinModelPortali P21517.
SMRi P21517. Positions 42-601.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10152N.
IntActi P21517. 8 interactions.
MINTi MINT-1219352.
STRINGi 511145.b0403.

Protein family/group databases

CAZyi CBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73506 ; AAC73506 ; b0403 .
BAE76183 ; BAE76183 ; BAE76183 .
GeneIDi 12934274.
949131.
KEGGi ecj:Y75_p0391.
eco:b0403.
PATRICi 32115955. VBIEscCol129921_0419.

Organism-specific databases

EchoBASEi EB0560.
EcoGenei EG10565. malZ.

Phylogenomic databases

eggNOGi COG0366.
HOGENOMi HOG000055363.
InParanoidi P21517.
KOi K01187.
OMAi GNNDPFC.

Enzyme and pathway databases

BioCyci EcoCyc:MALTODEXGLUCOSID-MONOMER.
ECOL316407:JW0393-MONOMER.
MetaCyc:MALTODEXGLUCOSID-MONOMER.

Miscellaneous databases

PROi P21517.

Gene expression databases

Genevestigatori P21517.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR015902. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF036918. Maltodextrin_glucosidase. 1 hit.
SMARTi SM00642. Aamy. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 123 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