| Identification |
|---|
| Name: | Maltodextrin glucosidase |
|---|
| Synonyms: | |
|---|
| Gene Name: | malZ |
|---|
| Enzyme Class: | |
|---|
| Biological Properties |
|---|
| General Function: | Involved in catalytic activity |
|---|
| Specific Function: | May play a role in regulating the intracellular level of maltotriose. Cleaves glucose from the reducing end of maltotriose and longer maltodextrins with a chain length of up to 7 glucose units |
|---|
| Cellular Location: | Cytoplasm |
|---|
| SMPDB Pathways: | |
|---|
| KEGG Pathways: | |
|---|
| KEGG Reactions: | | | |
1.0 | + | 1.0 | ↔ | 1.0D-Fructose | + | 1.0 |
| | |
1.0 | + | 1.0 | ↔ | 1.0beta-D-Fructose | + | 1.0 |
| | |
1.0Neohancoside D | + | 1.0 | ↔ | 1.0D-Fructose | + | 1.0 |
| | |
1.0Neohancoside D | + | 1.0 | ↔ | 1.0beta-D-Fructose | + | 1.0 |
| |
|
|---|
| SMPDB Reactions: | |
1.0 | + | 1.0 | ↔ | 1.0D-Fructose | + | 1.0 | + | 1.0 |
| |
|
|---|
| EcoCyc Reactions: | | | |
1.0a 1,4-α-D-glucan | + | 1.0 | → | 1.0a 1,4-α-D-glucan | + | 1.0 |
| |
|
|---|
| Complex Reactions: | |
|---|
| Metabolites: | |
|---|
| GO Classification: | | Function |
|---|
| binding | | catalytic activity | | cation binding | | hydrolase activity | | hydrolase activity, acting on glycosyl bonds | | hydrolase activity, hydrolyzing O-glycosyl compounds | | ion binding | | Process |
|---|
| carbohydrate metabolic process | | metabolic process | | primary metabolic process |
|
|---|
| Gene Properties |
|---|
| Blattner: | b0403 |
|---|
| Gene Orientation | Clockwise |
|---|
| Centisome Percentage: | 9.09 |
|---|
| Left Sequence End | 421742 |
|---|
| Right Sequence End | 423556 |
|---|
| Gene Sequence: | >1818 bp
ATGATGTTAAATGCATGGCACCTGCCGGTGCCCCCATTTGTTAAACAAAGCAAAGATCAA
CTGCTCATTACACTGTGGCTGACGGGCGAAGACCCACCGCAGCGCATTATGCTGCGTACA
GAACACGATAACGAAGAAATGTCAGTACCGATGCATAAGCAGCGCAGTCAGCCGCAGCCT
GGCGTCACCGCATGGCGTGCGGCGATTGATCTCTCCAGCGGACAACCCCGGCGGCGTTAC
AGTTTCAAACTGCTGTGGCACGATCGCCAGCGTTGGTTTACACCGCAGGGCTTCAGCCGA
ATGCCGCCGGCACGACTGGAGCAGTTTGCCGTCGATGTACCGGATATCGGCCCACAATGG
GCTGCGGATCAGATTTTTTATCAGATCTTCCCTGATCGTTTTGCGCGTAGTCTTCCTCGT
GAAGCTGAACAGGATCATGTCTATTACCATCATGCAGCCGGACAAGAGATCATCTTGCGT
GACTGGGATGAACCGGTCACGGCGCAGGCGGGCGGATCAACGTTCTATGGCGGCGATCTG
GACGGGATAAGCGAAAAACTGCCGTATCTGAAAAAGCTTGGCGTGACAGCGCTGTATCTC
AATCCGGTGTTTAAAGCTCCCAGCGTACATAAATACGATACCGAGGATTATCGCCATGTC
GATCCGCAGTTTGGCGGTGATGGGGCGTTGCTGCGTTTGCGACACAATACGCAGCAGCTG
GGAATGCGGCTGGTGCTGGACGGCGTGTTTAACCACAGTGGCGATTCCCATGCCTGGTTT
GACAGGCATAATCGTGGCACGGGTGGTGCTTGTCACAACCCCGAATCGCCCTGGCGCGAC
TGGTACTCGTTTAGTGATGATGGCACGGCGCTCGACTGGCTTGGCTATGCCAGCTTGCCG
AAGCTGGATTATCAGTCGGAAAGTCTGGTGAATGAAATTTATCGCGGGGAAGACAGTATT
GTCCGCCACTGGCTGAAAGCGCCGTGGAATATGGACGGCTGGCGGCTGGATGTGGTGCAT
ATGCTGGGGGAGGCGGGTGGGGCGCGCAATAATATGCAGCACGTTGCCGGGATCACCGAA
GCGGCGAAAGAAACCCAGCCGGAAGCGTATATTGTCGGCGAACATTTTGGCGATGCACGG
CAATGGTTACAGGCCGATGTGGAAGATGCCGCCATGAACTATCGTGGCTTCACATTCCCG
TTGTGGGGATTTCTTGCCAATACCGATATCTCTTACGATCCGCAGCAAATTGATGCCCAA
ACCTGTATGGCCTGGATGGATAATTACCGCGCAGGGCTTTCTCATCAACAACAATTACGT
ATGTTTAATCAGCTCGACAGCCACGATACTGCGCGATTTAAAACGCTGCTCGGTCGGGAT
ATTGCGCGCCTGCCGCTGGCGGTGGTCTGGCTGTTCACCTGGCCTGGTGTACCGTGCATT
TATTACGGTGATGAAGTAGGACTGGATGGCAAAAACGATCCGTTTTGCCGTAAACCGTTC
CCCTGGCAGGTGGAAAAGCAGGATACGGCGTTATTCGCGCTGTACCAGCGAATGATTGCG
CTGCGTAAGAAAAGTCAGGCGCTACGTCATGGCGGCTGTCAGGTGCTGTATGCGGAAGAT
AACGTGGTGGTATTTGTCCGCGTGCTGAATCAGCAACGTGTACTGGTGGCAATCAACCGT
GGCGAGGCCTGTGAAGTGGTGCTACCCGCGTCACCGTTTCTCAATGCCGTGCAATGGCAA
TGCAAAGAAGGGCATGGGCAACTGACTGACGGGATTCTGGCTTTGCCTGCCATTTCGGCT
ACGGTATGGATGAACTAA |
|---|
| Protein Properties |
|---|
| Pfam Domain Function: | |
|---|
| Protein Residues: | 605 |
|---|
| Protein Molecular Weight: | 69172 |
|---|
| Protein Theoretical pI: | 6 |
|---|
| Signaling Regions: | |
|---|
| Transmembrane Regions: | |
|---|
| Protein Sequence: | >Maltodextrin glucosidase
MMLNAWHLPVPPFVKQSKDQLLITLWLTGEDPPQRIMLRTEHDNEEMSVPMHKQRSQPQP
GVTAWRAAIDLSSGQPRRRYSFKLLWHDRQRWFTPQGFSRMPPARLEQFAVDVPDIGPQW
AADQIFYQIFPDRFARSLPREAEQDHVYYHHAAGQEIILRDWDEPVTAQAGGSTFYGGDL
DGISEKLPYLKKLGVTALYLNPVFKAPSVHKYDTEDYRHVDPQFGGDGALLRLRHNTQQL
GMRLVLDGVFNHSGDSHAWFDRHNRGTGGACHNPESPWRDWYSFSDDGTALDWLGYASLP
KLDYQSESLVNEIYRGEDSIVRHWLKAPWNMDGWRLDVVHMLGEAGGARNNMQHVAGITE
AAKETQPEAYIVGEHFGDARQWLQADVEDAAMNYRGFTFPLWGFLANTDISYDPQQIDAQ
TCMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKTLLGRDIARLPLAVVWLFTWPGVPCI
YYGDEVGLDGKNDPFCRKPFPWQVEKQDTALFALYQRMIALRKKSQALRHGGCQVLYAED
NVVVFVRVLNQQRVLVAINRGEACEVVLPASPFLNAVQWQCKEGHGQLTDGILALPAISA
TVWMN |
|---|
| References |
|---|
| External Links: | |
|---|
| General Reference: | - Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Reuter, K., Slany, R., Ullrich, F., Kersten, H. (1991). "Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes." J Bacteriol 173:2256-2264. Pubmed: 1706703
- Tapio, S., Yeh, F., Shuman, H. A., Boos, W. (1991). "The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase." J Biol Chem 266:19450-19458. Pubmed: 1918057
|
|---|
