Reviewed, UniProtKB/Swiss-Prot P21517 (MALZ_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	605 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.

Ontologies

Keywords
Biological process	Maltose metabolism
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	maltose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-glucosidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 605	605	Maltodextrin glucosidase		PRO_0000054334
Sites
	Active site	337	1	Nucleophile By similarity
	Active site	374	1	Proton donor By similarity
	Active site	449	1	By similarity
Experimental info
	Sequence conflict	302	1	L → M in CAA42498. Ref.1
	Sequence conflict	446	1	D → E in CAA42498. Ref.1
	Sequence conflict	547	1	R → S in CAA42498. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21517-1 [UniParc]. Last modified November 1, 1997. Version 4. Checksum: 80C200FDE11453EB	FASTA	605	69,172
	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

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: 1918057] [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: 9278503] [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: 16738553] [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: 1706703] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-605. Strain: K12.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X59839 Genomic DNA. Translation: CAA42498.1. Different initiation. U82664 Genomic DNA. Translation: AAB40159.1. U00096 Genomic DNA. Translation: AAC73506.1. AP009048 Genomic DNA. Translation: BAE76183.1. M37702 Genomic DNA. Translation: AAA16112.1.
PIR	C64769.
RefSeq	AP_001053.1. NP_414937.1.
3D structure databases
HSSP	HSSP built from PDB template 1EA9 based on UniProtKB Q59226.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:10152N.
Protein family/group databases
CAZy	CBM34. Carbohydrate-Binding Module Family 34. GH13. Glycoside Hydrolase Family 13.
Genome annotation databases
GeneID	949131.
GenomeReviews	Gene locus JW0393 in contig AP009048_GR. Gene locus b0403 in contig U00096_GR.
KEGG	ecj:JW0393. eco:b0403.
Organism-specific databases
EchoBASE	EB0560.
EcoGene	EG10565. malZ.
CMR	Search...
Phylogenomic databases
HOGENOM	P21517.
OMA	P21517. LKAPWSM.
Enzyme and pathway databases
BioCyc	EcoCyc:MALTODEXGLUCOSID-MON. MetaCyc:MALTODEXGLUCOSID-MON.
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]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 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]
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 1, 1997
Last modified:	June 16, 2009
This is version 80 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)