[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=1918057 [NCBI, ExPASy, EBI, Israel, Japan] Tapio S., Yeh F., Shuman H.A., Boos W.; "The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase."; J. Biol. Chem. 266:19450-19458(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; 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.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-605. STRAIN=K12; PubMed=1706703 [NCBI, ExPASy, EBI, Israel, Japan] Reuter K., Slany R., Ullrich F., Kersten H.; "Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes."; J. Bacteriol. 173:2256-2264(1991).

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: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
INDUCTION: Under positive control of malT.
SIMILARITY: Belongs to the glycosyl hydrolase 13 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X59839; CAA42498.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U82664; AAB40159.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73506.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76183.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M37702; AAA16112.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C64769; C64769.

RefSeq

AP_001053.1; -.
NP_414937.1; -.

3D structure databases

HSSP

Q59226; 1EA9. [HSSP ENTRY / PDB]

ModBase

P21517.

Protein-protein interaction databases

DIP

DIP:10152N; -.

Protein family/group databases

CAZy

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

Enzyme and pathway databases

BioCyc

EcoCyc:MALTODEXGLUCOSID-MON; -.
MetaCyc:MALTODEXGLUCOSID-MON; -.

Organism-specific databases

EchoBASE

EB0560; -.

EcoGene

EG10565; malZ.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004558;	Molecular function: alpha-glucosidase activity (inferred from electronic annotation from EC).
GO:0043169;	Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0000023;	Biological process: maltose metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006047; Glyco_hydro_13_cat.
IPR004185; Glyco_hydro_13_lg-like.
IPR006589; Glyco_hydro_13_sub_cat.
IPR013781; Glyco_hydro_sg_catalytic.
IPR017069; Maltodextrin_glucosidase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.80; Glyco_hydro_cat; 1.

Pfam

PF00128; Alpha-amylase; 1.
PF02903; Alpha-amylase_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036918; Maltodextrin_glucosidase; 1.

SMART

SM00642; Aamy; 1.
SMART graphical view of domain structure.

Genome annotation databases

GeneID

949131; -.

GenomeReviews

AP009048_GR; JW0393.
U00096_GR; b0403.

KEGG

ecj:JW0393; -.
eco:b0403; -.

Phylogenomic databases

HOGENOM

P21517; -.

OMA

P21517; LKAPWSM.

Genome annotation databases

CMR

P21517; b0403.

Other

ProtoNet

P21517.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Glycosidase; Hydrolase; Maltose metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 605`	`605`	`Maltodextrin glucosidase.`	`PRO_0000054334`
`ACT_SITE`	`337 337`		`Nucleophile (By similarity).`
`ACT_SITE`	`374 374`		`Proton donor (By similarity).`
`ACT_SITE`	`449 449`		`By similarity.`
`CONFLICT`	`302 302`		`L -> M (in Ref. 1; CAA42498).`
`CONFLICT`	`446 446`		`D -> E (in Ref. 1; CAA42498).`
`CONFLICT`	`547 547`		`R -> S (in Ref. 1; CAA42498).`

Sequence information

Length: 605 AA [This is the length of the unprocessed precursor]

Molecular weight: 69172 Da [This is the MW of the unprocessed precursor]

CRC64: 80C200FDE11453EB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMLNAWHLPV PPFVKQSKDQ LLITLWLTGE DPPQRIMLRT EHDNEEMSVP MHKQRSQPQP 

        70         80         90        100        110        120 
GVTAWRAAID LSSGQPRRRY SFKLLWHDRQ RWFTPQGFSR MPPARLEQFA VDVPDIGPQW 

       130        140        150        160        170        180 
AADQIFYQIF PDRFARSLPR EAEQDHVYYH HAAGQEIILR DWDEPVTAQA GGSTFYGGDL 

       190        200        210        220        230        240 
DGISEKLPYL KKLGVTALYL NPVFKAPSVH KYDTEDYRHV DPQFGGDGAL LRLRHNTQQL 

       250        260        270        280        290        300 
GMRLVLDGVF NHSGDSHAWF DRHNRGTGGA CHNPESPWRD WYSFSDDGTA LDWLGYASLP 

       310        320        330        340        350        360 
KLDYQSESLV NEIYRGEDSI VRHWLKAPWN MDGWRLDVVH MLGEAGGARN NMQHVAGITE 

       370        380        390        400        410        420 
AAKETQPEAY IVGEHFGDAR QWLQADVEDA AMNYRGFTFP LWGFLANTDI SYDPQQIDAQ 

       430        440        450        460        470        480 
TCMAWMDNYR AGLSHQQQLR MFNQLDSHDT ARFKTLLGRD IARLPLAVVW LFTWPGVPCI 

       490        500        510        520        530        540 
YYGDEVGLDG KNDPFCRKPF PWQVEKQDTA LFALYQRMIA LRKKSQALRH GGCQVLYAED 

       550        560        570        580        590        600 
NVVVFVRVLN QQRVLVAINR GEACEVVLPA SPFLNAVQWQ CKEGHGQLTD GILALPAISA 


TVWMN

P21517 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools