Reviewed,
UniProtKB/Swiss-Prot P26612 (AMY2_ECOLI)
Last modified
June 16, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytoplasmic alpha-amylase EC=3.2.1.1 Alternative name(s): 1,4-alpha-D-glucan glucanohydrolase | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 495 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred 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 | |
| Sequence similarities | Belongs to the glycosyl hydrolase 13 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Cellular component | Cytoplasm |
| Ligand | Calcium Metal-binding |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 495 | 495 | Cytoplasmic alpha-amylase | PRO_0000054287 | |||||
Sites | |||||||||
| Active site | 235 | 1 | Nucleophile By similarity | ||||||
| Active site | 265 | 1 | Proton donor By similarity | ||||||
| Active site | 332 | 1 | By similarity | ||||||
| Metal binding | 104 | 1 | Calcium By similarity | ||||||
| Metal binding | 239 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 19 – 20 | 2 | KL → SS in AAA23810. Ref.1 | ||||||
| Sequence conflict | 109 | 1 | A → V in AAA23810. Ref.1 | ||||||
| Sequence conflict | 149 | 1 | Q → E in AAA23810. Ref.1 | ||||||
| Sequence conflict | 234 | 1 | L → I in AAA23810. Ref.1 | ||||||
Sequences
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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. 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. | |
| PIR | A45738. D64956. |
| RefSeq | AP_002542.1. NP_416437.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HVX based on UniProtKB P06279. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:9108N. |
Protein family/group databases | |
| CAZy | GH13. Glycoside Hydrolase Family 13. |
Genome annotation databases | |
| GeneID | 946434. |
| GenomeReviews | Gene locus JW1912 in contig AP009048_GR. Gene locus b1927 in contig U00096_GR. |
| KEGG | ecj:JW1912. eco:b1927. |
Organism-specific databases | |
| EchoBASE | EB1360. |
| EcoGene | EG11387. amyA. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P26612. |
| OMA | P26612. VWIPPAY. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:ALPHA-AMYL-CYTO-MON. MetaCyc:ALPHA-AMYL-CYTO-MON. |
Family and domain databases | |
| InterPro | IPR006048. 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] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| Pfam | PF00128. Alpha-amylase. 1 hit. PF02806. Alpha-amylase_C. 1 hit. [Graphical view] |
| PIRSF | PIRSF001021. Alph-amls_thrmst. 1 hit. |
| SMART | SM00642. Aamy. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMY2_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P26612 Secondary accession number(s): P78072 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (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 |

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