Maltodextrin glucosidase - Escherichia coli (strain K12)

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P21517 (MALZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Maltodextrin glucosidase
EC=3.2.1.20

Alternative name(s):
Alpha-glucosidase

Gene names

Name:	malZ
Ordered Locus Names:	b0403, JW0393

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	604 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 activity	Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Induction	Under positive control of MalT.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.
Sequence caution	The sequence AAB40159.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAE76183.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Maltose metabolism
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alpha-glucan catabolic process Inferred from direct assay Ref.1. Source: EcoCyc cellular oligosaccharide catabolic process Inferred from mutant phenotype PubMed 16321936. Source: EcoCyc maltose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 3512530. Source: EcoCyc
Molecular_function	alpha-glucosidase activity Inferred from direct assay Ref.1. Source: EcoCyc cation binding Inferred from electronic annotation. Source: InterPro maltose alpha-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 604

604

Maltodextrin glucosidase

PRO_0000054334

Sites

Active site

336

Nucleophile By similarity

Active site

373

Proton donor By similarity

Site

448

Transition state stabilizer By similarity

Experimental info

Sequence conflict

301

L → M in CAA42498. Ref.1

Sequence conflict

445

D → E in CAA42498. Ref.1

Sequence conflict

546

R → S in CAA42498. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P21517 [UniParc].

Last modified November 16, 2011. Version 5.
Checksum: B5A14754D7A42CCB
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FASTA

604

69,041

        10         20         30         40         50         60 
MLNAWHLPVP PFVKQSKDQL LITLWLTGED PPQRIMLRTE HDNEEMSVPM HKQRSQPQPG 

        70         80         90        100        110        120 
VTAWRAAIDL SSGQPRRRYS FKLLWHDRQR WFTPQGFSRM PPARLEQFAV DVPDIGPQWA 

       130        140        150        160        170        180 
ADQIFYQIFP DRFARSLPRE AEQDHVYYHH AAGQEIILRD WDEPVTAQAG GSTFYGGDLD 

       190        200        210        220        230        240 
GISEKLPYLK KLGVTALYLN PVFKAPSVHK YDTEDYRHVD PQFGGDGALL RLRHNTQQLG 

       250        260        270        280        290        300 
MRLVLDGVFN HSGDSHAWFD RHNRGTGGAC HNPESPWRDW YSFSDDGTAL DWLGYASLPK 

       310        320        330        340        350        360 
LDYQSESLVN EIYRGEDSIV RHWLKAPWNM DGWRLDVVHM LGEAGGARNN MQHVAGITEA 

       370        380        390        400        410        420 
AKETQPEAYI VGEHFGDARQ WLQADVEDAA MNYRGFTFPL WGFLANTDIS YDPQQIDAQT 

       430        440        450        460        470        480 
CMAWMDNYRA GLSHQQQLRM FNQLDSHDTA RFKTLLGRDI ARLPLAVVWL FTWPGVPCIY 

       490        500        510        520        530        540 
YGDEVGLDGK NDPFCRKPFP WQVEKQDTAL FALYQRMIAL RKKSQALRHG GCQVLYAEDN 

       550        560        570        580        590        600 
VVVFVRVLNQ QRVLVAINRG EACEVVLPAS PFLNAVQWQC KEGHGQLTDG ILALPAISAT 


VWMN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	C64769.
RefSeq	NP_414937.2. NC_000913.2. YP_488695.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P21517.
SMR	P21517. Positions 4-601.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10152N.
IntAct	P21517. 8 interactions.
MINT	MINT-1219352.
STRING	511145.b0403.
Protein family/group databases
CAZy	CBM34. Carbohydrate-Binding Module Family 34. GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73506; AAC73506; b0403. BAE76183; BAE76183; BAE76183.
GeneID	12934274. 949131.
KEGG	ecj:Y75_p0391. eco:b0403.
PATRIC	32115955. VBIEscCol129921_0419.
Organism-specific databases
EchoBASE	EB0560.
EcoGene	EG10565. malZ.
Phylogenomic databases
eggNOG	COG0366.
HOGENOM	HOG000055363.
KO	K01187.
OMA	CQVIYAE.
ProtClustDB	PRK10785.
Enzyme and pathway databases
BioCyc	EcoCyc:MALTODEXGLUCOSID-MONOMER. ECOL316407:JW0393-MONOMER. MetaCyc:MALTODEXGLUCOSID-MONOMER.
Gene expression databases
Genevestigator	P21517.
Family and domain databases
Gene3D	2.60.40.1180. 1 hit. 3.20.20.80. 1 hit.
InterPro	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]
PANTHER	PTHR10357. PTHR10357. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02903. Alpha-amylase_N. 1 hit. [Graphical view]
PIRSF	PIRSF036918. Maltodextrin_glucosidase. 1 hit.
SMART	SM00642. Aamy. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit. SSF81296. Ig_E-set. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MALZ_ECOLI

Accession

Primary (citable) accession number: P21517
Secondary accession number(s): Q2MC23

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	November 16, 2011
Last modified:	May 1, 2013
This is version 116 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents