P25718 (AMY1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase
EC=3.2.1.1

Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase

Gene names

Name:	malS
Ordered Locus Names:	b3571, JW3543

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	676 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Since only maltooligosaccharides up to a chain length of 6 glucose units are actively transported through the cytoplasmic membrane via the membrane-bound complex of three proteins, MalF, MalG, and MalK, longer maltooligosaccharides must first be degraded by the periplasmic alpha-amylase, the MalS protein.
Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Monomer.
Subcellular location	Periplasm.
Induction	Under the regulatory control of the MalT protein.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Periplasm
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Ref.1
	Chain	18 – 676	659	Alpha-amylase		PRO_0000001339
Sites
	Active site	460	1	Nucleophile By similarity
	Active site	503	1	Proton donor By similarity
	Metal binding	314	1	Calcium By similarity
	Metal binding	464	1	Calcium; via carbonyl oxygen By similarity
	Site	565	1	Transition state stabilizer By similarity
Amino acid modifications
	Disulfide bond	57 ↔ 75		Ref.5
	Disulfide bond	121 ↔ 537		Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P25718 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 980110EFA45E011D	FASTA	676	75,713
	10 20 30 40 50 60 MKLAACFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP 70 80 90 100 110 120 ADAIKLNQML SLQPCSNTPP QWRLFRDGEY TLQIDTRSGT PTLMISIQNA AEPVASLVRE 130 140 150 160 170 180 CPKWDGLPLT VDVSATFPEG AAVRDYYSQQ IAIVKNGQIM LQPAATSNGL LLLERAETDT 190 200 210 220 230 240 SAPFDWHNAT VYFVLTDRFE NGDPSNDQSY GRHKDGMAEI GTFHGGDLRG LTNKLDYLQQ 250 260 270 280 290 300 LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGNE ADLRTLVDSA 310 320 330 340 350 360 HQRGIRILFD VVMNHTGYAT LADMQEYQFG ALYLSGDEVK KSLGERWSDW KPAAGQTWHS 370 380 390 400 410 420 FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STTASGLPVF 430 440 450 460 470 480 YKNKMDTHAK AIDGYTPRDY LTHWLSQWVR DYGIDGFRVD TAKHVELPAW QQLKTEASAA 490 500 510 520 530 540 LREWKKANPD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ 550 560 570 580 590 600 MDTTWQQMAE KLQGFNVLSY LSSHDTRLFR EGGDKAAELL LLAPGAVQIF YGDESSRPFG 610 620 630 640 650 660 PTGSDPLQGT RSDMNWQDVS GKSAASVAHW QKISQFRARH PAIGAGKQTT LLLKQGYGFV 670 REHGDDKVLV VWAGQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of the MalT-dependent periplasmic alpha-amylase of Escherichia coli encoded by malS." Schneider E., Freundlieb S., Tapio S., Boos W. J. Biol. Chem. 267:5148-5154(1992) [PubMed: 1544897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-43. Strain: K12.
[2]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract] 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]	"Biochemical characterization and mass spectrometric disulfide bond mapping of periplasmic alpha-amylase MalS of Escherichia coli." Spiess C., Happersberger H.P., Glocker M.O., Spiess E., Rippe K., Ehrmann M. J. Biol. Chem. 272:22125-22133(1997) [PubMed: 9268356] [Abstract] Cited for: DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58994 Genomic DNA. Translation: CAA41740.1. U00039 Genomic DNA. Translation: AAB18548.1. U00096 Genomic DNA. Translation: AAC76595.1. AP009048 Genomic DNA. Translation: BAE77722.1.
PIR	S23807.
RefSeq	NP_418028.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P25718.
SMR	P25718. Positions 181-673.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10148N.
IntAct	P25718. 1 interaction.
MINT	MINT-1293484.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000002245; EBESCP00000002245; EBESCG00000001840. EBESCT00000016789; EBESCP00000016080; EBESCG00000015848.
GeneID	948088.
GenomeReviews	Gene locus JW3543 in contig AP009048_GR. Gene locus b3571 in contig U00096_GR.
KEGG	ecj:JW3543. eco:b3571.
PATRIC	32122618. VBIEscCol129921_3686.
Organism-specific databases
EchoBASE	EB1292.
EcoGene	EG11316. malS.
Phylogenomic databases
eggNOG	COG0366.
GeneTree	EBGT00050000009459.
HOGENOM	HBG298608.
OMA	RISQFRA.
PhylomeDB	P25718.
ProtClustDB	PRK09505.
Enzyme and pathway databases
BioCyc	EcoCyc:ALPHA-AMYL-PERI-MONOMER. MetaCyc:ALPHA-AMYL-PERI-MONOMER.
Gene expression databases
Genevestigator	P25718.
Family and domain databases
InterPro	IPR014635. A_amylase_MalS. IPR015902. Alpha_amylase. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
KO	K01176.
PANTHER	PTHR10357. Alpha_amylase. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. [Graphical view]
PIRSF	PIRSF036917. Alph_amls_MalS. 1 hit.
SMART	SM00642. Aamy. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMY1_ECOLI

Accession

Primary (citable) accession number: P25718
Secondary accession number(s): Q2M7N4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	January 25, 2012
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program