Reviewed,
UniProtKB/Swiss-Prot P77791 (MAA_ECOLI)
Last modified
June 16, 2009.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Maltose O-acetyltransferase EC=2.3.1.79 Alternative name(s): Maltose transacetylase | ||||||
| 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 | 183 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 | Acetylates maltose and other sugars. |
| Catalytic activity | Acetyl-CoA + maltose = CoA + acetyl-maltose. |
| Subunit structure | Homodimer. |
| Sequence similarities | Belongs to the transferase hexapeptide repeat family. |
| biophysicochemical properties | Kinetic parameters: Acetylates glucose, maltose, mannose, galactose, and fructose with a decreasing relative rate of 1, 0.55, 0.20, 0.07, 0.04. KM=62 mM for glucose KM=90 mM for maltose Vmax=0.20 mmol/min/mg enzyme with glucose as substrate Vmax=0.11 mmol/min/mg enzyme with maltose as substrate |
Ontologies
| Keywords | |
|---|---|
| Domain | Repeat |
| Molecular function | Transferase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular function | maltose O-acetyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.5 | ||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 183 | 182 | Maltose O-acetyltransferase | PRO_0000068729 | |||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Helix | 4 – 9 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 19 – 37 | 19 | |||||||||||||||||||||||||||||||||||||||
| Helix | 43 – 53 | 11 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 54 – 56 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 58 – 62 | 5 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 66 – 71 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 74 – 76 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 82 | 5 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 84 – 89 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 94 – 96 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 107 – 109 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 117 – 120 | 4 | |||||||||||||||||||||||||||||||||||||||
| Turn | 121 – 123 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 125 – 127 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 130 – 132 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 168 – 173 | 6 | |||||||||||||||||||||||||||||||||||||||
| Turn | 174 – 177 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 178 – 182 | 5 | |||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Boehm A.S. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574. |
| [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] | "Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [6] | "Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural, gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20,000." Brand B., Boos W. J. Biol. Chem. 266:14113-14118(1991) [PubMed: 1856235] [Abstract] Cited for: CHARACTERIZATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AJ223173 Genomic DNA. Translation: CAA11147.1. U82664 Genomic DNA. Translation: AAB40214.1. U00096 Genomic DNA. Translation: AAC73561.1. AP009048 Genomic DNA. Translation: BAE76238.1. | |||||||||||||
| PIR | B64776. | ||||||||||||
| RefSeq | AP_001108.1. NP_414992.1. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP:10140N. | ||||||||||||
2-D gel databases | |||||||||||||
| SWISS-2DPAGE | P77791. | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 945096. | ||||||||||||
| GenomeReviews | Gene locus JW0448 in contig AP009048_GR. Gene locus b0459 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW0448. eco:b0459. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB3990. | ||||||||||||
| EcoGene | EG14239. maa. | ||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P77791. | ||||||||||||
| OMA | P77791. AVIRPPF. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:MALTACETYLTRAN-MON. MetaCyc:MALTACETYLTRAN-MON. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. [Graphical view] | ||||||||||||
| Pfam | PF00132. Hexapep. 3 hits. [Graphical view] | ||||||||||||
| PROSITE | PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | MAA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P77791 Secondary accession number(s): Q2MBW8 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


