Identification |
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Name: | Maltodextrin glucosidase |
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Synonyms: | |
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Gene Name: | malZ |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in catalytic activity |
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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 |
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Cellular Location: | Cytoplasm |
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SMPDB Pathways: | |
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KEGG Pathways: | |
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KEGG Reactions: | | | |
1.0 | + | 1.0 | ↔ | 1.0D-Fructose | + | 1.0 |
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1.0 | + | 1.0 | ↔ | 1.0beta-D-Fructose | + | 1.0 |
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1.0Neohancoside D | + | 1.0 | ↔ | 1.0D-Fructose | + | 1.0 |
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1.0Neohancoside D | + | 1.0 | ↔ | 1.0beta-D-Fructose | + | 1.0 |
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SMPDB Reactions: | |
1.0 | + | 1.0 | ↔ | 1.0D-Fructose | + | 1.0 | + | 1.0 |
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EcoCyc Reactions: | | | |
1.0a 1,4-α-D-glucan | + | 1.0 | → | 1.0a 1,4-α-D-glucan | + | 1.0 |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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binding | catalytic activity | cation binding | hydrolase activity | hydrolase activity, acting on glycosyl bonds | hydrolase activity, hydrolyzing O-glycosyl compounds | ion binding | Process |
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carbohydrate metabolic process | metabolic process | primary metabolic process |
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Gene Properties |
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Blattner: | b0403 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 9.09 |
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Left Sequence End | 421742 |
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Right Sequence End | 423556 |
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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 |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 605 |
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Protein Molecular Weight: | 69172 |
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Protein Theoretical pI: | 6 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Maltodextrin glucosidase
MMLNAWHLPVPPFVKQSKDQLLITLWLTGEDPPQRIMLRTEHDNEEMSVPMHKQRSQPQP
GVTAWRAAIDLSSGQPRRRYSFKLLWHDRQRWFTPQGFSRMPPARLEQFAVDVPDIGPQW
AADQIFYQIFPDRFARSLPREAEQDHVYYHHAAGQEIILRDWDEPVTAQAGGSTFYGGDL
DGISEKLPYLKKLGVTALYLNPVFKAPSVHKYDTEDYRHVDPQFGGDGALLRLRHNTQQL
GMRLVLDGVFNHSGDSHAWFDRHNRGTGGACHNPESPWRDWYSFSDDGTALDWLGYASLP
KLDYQSESLVNEIYRGEDSIVRHWLKAPWNMDGWRLDVVHMLGEAGGARNNMQHVAGITE
AAKETQPEAYIVGEHFGDARQWLQADVEDAAMNYRGFTFPLWGFLANTDISYDPQQIDAQ
TCMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKTLLGRDIARLPLAVVWLFTWPGVPCI
YYGDEVGLDGKNDPFCRKPFPWQVEKQDTALFALYQRMIALRKKSQALRHGGCQVLYAED
NVVVFVRVLNQQRVLVAINRGEACEVVLPASPFLNAVQWQCKEGHGQLTDGILALPAISA
TVWMN |
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References |
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External Links: | |
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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
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