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ECOLI:MALQ
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | malQ (synonyms: malA) | |
| Protein Name(s) | 4-alpha-glucanotransferase
Amylomaltase Disproportionating enzyme D-enzyme | |
| External Links | ||
| UniProt | P15977 | |
| EMBL | M32793 U18997 U00096 AP009048 | |
| PIR | C65137 | |
| RefSeq | NP_417875.1 YP_492016.1 | |
| ProteinModelPortal | P15977 | |
| SMR | P15977 | |
| DIP | DIP-10147N | |
| IntAct | P15977 | |
| MINT | MINT-1275716 | |
| STRING | 511145.b3416 | |
| CAZy | GH77 | |
| PaxDb | P15977 | |
| PRIDE | P15977 | |
| EnsemblBacteria | AAC76441 BAE77875 | |
| GeneID | 12932222 947923 | |
| KEGG | ecj:Y75_p3760 eco:b3416 | |
| PATRIC | 32122270 | |
| EchoBASE | EB0556 | |
| EcoGene | EG10561 | |
| eggNOG | COG1640 | |
| HOGENOM | HOG000245168 | |
| InParanoid | P15977 | |
| KO | K00705 | |
| OMA | WSRQDEL | |
| OrthoDB | EOG6SR926 | |
| PhylomeDB | P15977 | |
| BioCyc | EcoCyc:AMYLOMALT-MONOMER ECOL316407:JW3379-MONOMER MetaCyc:AMYLOMALT-MONOMER | |
| PRO | PR:P15977 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P15977 | |
| GO | GO:0005829 GO:0004134 GO:0005977 GO:0000025 | |
| Gene3D | 3.20.20.80 | |
| InterPro | IPR003385 IPR013781 IPR017853 | |
| Pfam | PF02446 | |
| SUPFAM | SSF51445 | |
| TIGRFAMs | TIGR00217 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0000023 |
maltose metabolic process |
ECO:0000315 |
P |
Figure 6 |
complete | |||||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004134 |
4-alpha-glucanotransferase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004134 |
4-alpha-glucanotransferase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0000025 |
maltose catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0000025 |
maltose catabolic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0000025 |
maltose catabolic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0005977 |
glycogen metabolic process |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004134 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0005977 |
glycogen metabolic process |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0004134 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0005977 |
glycogen metabolic process |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0004134 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0005977 |
glycogen metabolic process |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004134 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004134 |
4-alpha-glucanotransferase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0005975 |
carbohydrate metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004134 |
4-alpha-glucanotransferase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0102500 |
beta-maltose 4-alpha-glucanotransferase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0005975 |
carbohydrate metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016757 |
transferase activity, transferring glycosyl groups |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Lengsfeld, C et al. (2009) Glucose- and glucokinase-controlled mal gene expression in Escherichia coli. J. Bacteriol. 191 701-12 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
- ↑ WIESMEYER, H & COHN, M (1960) The characterization of the pathway of maltose utilization by Escherichia coli. I. Purification and physical chemical properties of the enzyme amylomaltase. Biochim. Biophys. Acta 39 417-26 PubMed GONUTS page
- ↑ 5.0 5.1 Palmer, TN et al. (1976) The action pattern of amylomaltase from Escherichia coli. Eur. J. Biochem. 69 105-15 PubMed GONUTS page
- ↑ 6.0 6.1 WIESMEYER, H & COHN, M (1960) The characterization of the pathway of maltose utilization by Escherichia coli. II. General properties and mechanism of action of amylomaltase. Biochim. Biophys. Acta 39 427-39 PubMed GONUTS page
- ↑ Hatfield, D et al. (1969) Genetic analysis of the maltose A region in Escherichia coli. J. Bacteriol. 98 559-67 PubMed GONUTS page
