Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P26612 (AMY2_ECOLI)

Last modified June 16, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytoplasmic alpha-amylase
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
Gene names
Name: amyA
Synonyms: yedC
Ordered Locus Names: b1927, JW1912
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Cytoplasmic alpha-amylase
PRO_0000054287

Sites

Active site2351Nucleophile By similarity
Active site2651Proton donor By similarity
Active site3321 By similarity
Metal binding1041Calcium By similarity
Metal binding2391Calcium; via carbonyl oxygen By similarity

Experimental info

Sequence conflict19 – 202KL → SS in AAA23810. Ref.1
Sequence conflict1091A → V in AAA23810. Ref.1
Sequence conflict1491Q → E in AAA23810. Ref.1
Sequence conflict2341L → I in AAA23810. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P26612-1 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 26AFF6797DDA54D6

FASTA49556,639
        10         20         30         40         50         60 
MRNPTLLQCF HWYYPEGGKL WPELAERADG FNDIGINMVW LPPAYKGASG GYSVGYDSYD 

        70         80         90        100        110        120 
LFDLGEFDQK GSIPTKYGDK AQLLAAIDAL KRNDIAVLLD VVVNHKMGAD EKEAIRVQRV 

       130        140        150        160        170        180 
NADDRTQIDE EIIECEGWTR YTFPARAGQY SQFIWDFKCF SGIDHIENPD EDGIFKIVND 

       190        200        210        220        230        240 
YTGEGWNDQV DDELGNFDYL MGENIDFRNH AVTEEIKYWA RWVMEQTQCD GFRLDAVKHI 

       250        260        270        280        290        300 
PAWFYKEWIE HVQEVAPKPL FIVAEYWSHE VDKLQTYIDQ VEGKTMLFDA PLQMKFHEAS 

       310        320        330        340        350        360 
RMGRDYDMTQ IFTGTLVEAD PFHAVTLVAN HDTQPLQALE APVEPWFKPL AYALILLREN 

       370        380        390        400        410        420 
GVPSVFYPDL YGAHYEDVGG DGQTYPIDMP IIEQLDELIL ARQRFAHGVQ TLFFDHPNCI 

       430        440        450        460        470        480 
AFSRSGTDEF PGCVVVMSNG DDGEKTIHLG ENYGNKTWRD FLGNRQERVV TDENGEATFF 

       490 
CNGGSVSVWV IEEVI 

« Hide

References

« Hide 'large scale' references
[1]"Escherichia coli produces a cytoplasmic alpha-amylase, AmyA."
Raha M., Kawagishi I., Mueller V., Kihara M., Macnab R.M.
J. Bacteriol. 174:6644-6652(1992) [PubMed: 1400215] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: JA11.
[2]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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]"Subdivision of flagellar region III of the Escherichia coli and Salmonella typhimurium chromosomes and identification of two additional flagellar genes."
Kawagishi I., Mueller V., Williams A.W., Irikura V.M., Macnab R.M.
J. Gen. Microbiol. 138:1051-1065(1992) [PubMed: 1527488] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
Strain: JA11.
[6]"Organization of the Escherichia coli and Salmonella typhimurium chromosomes between flagellar regions IIIa and IIIb, including a large non-coding region."
Raha M., Kihara M., Kawagishi I., Macnab R.M.
J. Gen. Microbiol. 139:1401-1407(1993) [PubMed: 8371104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 475-495.
Strain: JA11.

Cross-references

Sequence databases

L01642 Genomic DNA. Translation: AAA23810.1.
U00096 Genomic DNA. Translation: AAC74994.1.
AP009048 Genomic DNA. Translation: BAA15755.1.
M85240 Genomic DNA. No translation available.
L13279 Genomic DNA. Translation: AAA82575.1.
PIRA45738. D64956.
RefSeqAP_002542.1.
NP_416437.1.

3D structure databases

HSSPHSSP built from PDB template 1HVX based on UniProtKB P06279.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9108N.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Genome annotation databases

GeneID946434.
GenomeReviewsGene locus JW1912 in contig AP009048_GR.
Gene locus b1927 in contig U00096_GR.
KEGGecj:JW1912.
eco:b1927.

Organism-specific databases

EchoBASEEB1360.
EcoGeneEG11387. amyA.
CMRSearch...

Phylogenomic databases

HOGENOMP26612.
OMAP26612. VWIPPAY.

Enzyme and pathway databases

BioCycEcoCyc:ALPHA-AMYL-CYTO-MON.
MetaCyc:ALPHA-AMYL-CYTO-MON.

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR013776. A-amylase_thermo.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PIRSFPIRSF001021. Alph-amls_thrmst. 1 hit.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMY2_ECOLI
AccessionPrimary (citable) accession number: P26612
Secondary accession number(s): P78072
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents