Maltodextrin phosphorylase (P00490)

Identification
Name:Maltodextrin phosphorylase
Synonyms:Not Available
Gene Name:malP
Enzyme Class:
Biological Properties
General Function:Involved in phosphorylase activity
Specific Function:Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties
Cellular Location:Not Available
SMPDB Pathways:
  • Secondary metabolites: Trehalose Biosynthesis and Metabolism PW000968
  • Starch and sucrose metabolism PW000941
KEGG Pathways:
KEGG Reactions:
1.0Starch+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Starch + 1.0Phosphate ↔ 1.01,4-alpha-D-glucan + 1.0Glucose 1-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb
1.0Phosphate ↔ 1.0Glucose 1-phosphate
ReactionCard
SMPDB Reactions:
1.0Alpha-D-glucose 1-phosphate+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Alpha-D-glucose 1-phosphate + 1.0Amylose ↔ 1.0Phosphate + 1.0Glycogen
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Alpha-D-glucose 1-phosphate
1.0Maltotetraose + 1.0Phosphate → 1.0Maltotriose + 1.0Alpha-D-glucose 1-phosphate
ReactionCard
Complex Reactions:
1.0branching glycogen+1.0Thumb → 1.0Thumb
1.0branching glycogen + 1.0Phosphate → 1.0Glucose 1-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb
1.0Glycogen + 1.0Phosphate → 1.0Glucose 1-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Maltoheptaose + 1.0Phosphate ↔ 1.0Glucose 1-phosphate + 1.0Maltohexaose
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Maltohexaose + 1.0Phosphate ↔ 1.0Glucose 1-phosphate + 1.0Maltopentaose
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Maltopentaose + 1.0Phosphate ↔ 1.0Glucose 1-phosphate + 1.0Maltotetraose
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211101,4-alpha-D-glucanMetaboCard
ECMDB24082AmyloseMetaboCard
ECMDB01586Glucose 1-phosphateMetaboCard
ECMDB21341GlycogenMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB20349MaltoheptaoseMetaboCard
ECMDB21243MaltohexaoseMetaboCard
ECMDB21244MaltopentaoseMetaboCard
ECMDB01296MaltotetraoseMetaboCard
ECMDB01262MaltotrioseMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Function
binding
catalytic activity
cofactor binding
phosphorylase activity
pyridoxal phosphate binding
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring hexosyl groups
Process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b3417
Gene OrientationCounterclockwise
Centisome Percentage:76.47
Left Sequence End3548102
Right Sequence End3550495
Gene Sequence:
>2394 bp
ATGTCACAACCTATTTTTAACGATAAGCAATTTCAGGAAGCGCTTTCACGTCAGTGGCAG
CGTTATGGCTTAAATTCTGCGGCTGAAATGACTCCTCGCCAGTGGTGGCTAGCAGTGAGT
GAAGCACTGGCCGAAATGCTGCGTGCTCAGCCATTCGCCAAGCCGGTGGCGAATCAGCGA
CATGTTAACTACATCTCAATGGAGTTTTTGATTGGTCGCCTGACGGGCAACAACCTGTTG
AATCTCGGCTGGTATCAGGATGTACAGGATTCGTTGAAGGCTTATGACATCAATCTGACG
GACCTGCTGGAAGAAGAGATCGACCCGGCGCTGGGTAACGGTGGTCTGGGACGTCTGGCG
GCGTGCTTCCTCGACTCAATGGCAACTGTCGGTCAGTCTGCGACGGGTTACGGTCTGAAC
TATCAATATGGTTTGTTCCGCCAGTCTTTTGTCGATGGCAAACAGGTTGAAGCGCCGGAT
GACTGGCATCGCAGTAACTACCCGTGGTTCCGCCACAACGAAGCACTGGATGTGCAGGTA
GGGATTGGCGGTAAAGTGACGAAAGACGGACGCTGGGAGCCGGAGTTTACCATTACCGGT
CAAGCGTGGGATCTCCCCGTTGTCGGCTATCGTAATGGCGTGGCGCAGCCGCTGCGTCTG
TGGCAGGCGACGCACGCGCATCCGTTTGATCTGACTAAATTTAACGACGGTGATTTCTTG
CGTGCCGAACAGCAGGGCATCAATGCGGAAAAACTGACCAAAGTTCTCTATCCAAACGAC
AACCATACTGCCGGTAAAAAGCTGCGCCTGATGCAGCAATACTTCCAGTGTGCCTGTTCG
GTAGCGGATATTTTGCGTCGCCATCATCTGGCGGGGCGTAAACTGCACGAACTGGCGGAT
TACGAAGTTATTCAGCTGAACGATACCCACCCAACTATCGCGATTCCAGAACTGCTGCGC
GTGCTGATCGATGAGCACCAGATGAGCTGGGATGACGCCTGGGCCATTACCAGCAAAACT
TTCGCTTACACCAACCATACCCTGATGCCAGAAGCGCTGGAACGCTGGGATGTGAAACTG
GTGAAAGGCTTACTGCCGCGCCACATGCAGATTATTAACGAAATTAATACTCGCTTTAAA
ACGCTGGTAGAGAAAACCTGGCCGGGCGATGAAAAAGTGTGGGCCAAACTGGCGGTGGTG
CACGACAAACAAGTGCATATGGCGAACCTGTGTGTGGTTGGCGGTTTCGCGGTGAACGGT
GTTGCGGCGCTGCACTCGGATCTGGTGGTGAAAGATCTGTTCCCGGAATATCACCAGCTA
TGGCCGAACAAATTCCATAACGTCACCAACGGTATTACCCCACGTCGCTGGATCAAACAG
TGCAACCCGGCACTGGCGGCTCTGTTGGATAAATCACTGCAAAAAGAGTGGGCTAACGAT
CTCGATCAGCTGATCAATCTGGAAAAATTCGCTGATGATGCGAAATTCCGTCAGCAATAT
CGCGAGATCAAGCAGGCGAATAAAGTCCGTCTGGCGGAGTTTGTGAAAGTTCGTACCGGT
ATTGAGATCAATCCACAGGCGATTTTCGATATTCAGATCAAACGTTTGCATGAGTACAAA
CGCCAGCACCTGAATCTGCTGCATATTCTGGCGTTGTACAAAGAAATTCGTGAAAACCCG
CAGGCTGATCGCGTACCGCGCGTCTTCCTCTTCGGCGCGAAAGCGGCACCGGGCTACTAC
CTGGCGAAGAATATTATCTTTGCGATCAACAAAGTGGCTGACGTGATCAACAACGATCCG
CTGGTTGGCGATAAGTTGAAGGTGGTGTTCCTGCCGGATTATTGCGTTTCGGCGGCGGAA
AAACTGATCCCGGCGGCGGATATCTCCGAACAAATTTCGACTGCAGGTAAAGAAGCTTCC
GGTACCGGCAATATGAAACTGGCGCTCAATGGTGCGCTTACTGTCGGTACGCTGGATGGG
GCGAACGTTGAAATCGCCGAGAAAGTCGGTGAAGAAAATATCTTTATTTTTGGTCATACC
GTGGAACAAGTGAAGGCAATTCTGGCCAAAGGCTACGACCCGGTGAAATGGCGGAAGAAA
GATAAGGTGCTGGACGCAGTATTGAAAGAGCTGGAAAGCGGTAAATACAGCGACGGCGAT
AAGCATGCCTTCGACCAGATGCTGCACAGTATCGGCAAACAGGGCGGCGATCCGTATCTG
GTGATGGCGGATTTCGCAGCCTATGTAGAGGCACAAAAGCAGGTGGATGTGCTGTACCGC
GACCAGGAGGCCTGGACTCGCGCGGCGATCCTCAATACCGCCCGCTGCGGTATGTTTAGC
TCGGATCGCTCTATTCGCGATTATCAGGCTCGTATCTGGCAGGCAAAACGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:797
Protein Molecular Weight:90522
Protein Theoretical pI:7
PDB File:1QM5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Maltodextrin phosphorylase
MSQPIFNDKQFQEALSRQWQRYGLNSAAEMTPRQWWLAVSEALAEMLRAQPFAKPVANQR
HVNYISMEFLIGRLTGNNLLNLGWYQDVQDSLKAYDINLTDLLEEEIDPALGNGGLGRLA
ACFLDSMATVGQSATGYGLNYQYGLFRQSFVDGKQVEAPDDWHRSNYPWFRHNEALDVQV
GIGGKVTKDGRWEPEFTITGQAWDLPVVGYRNGVAQPLRLWQATHAHPFDLTKFNDGDFL
RAEQQGINAEKLTKVLYPNDNHTAGKKLRLMQQYFQCACSVADILRRHHLAGRKLHELAD
YEVIQLNDTHPTIAIPELLRVLIDEHQMSWDDAWAITSKTFAYTNHTLMPEALERWDVKL
VKGLLPRHMQIINEINTRFKTLVEKTWPGDEKVWAKLAVVHDKQVHMANLCVVGGFAVNG
VAALHSDLVVKDLFPEYHQLWPNKFHNVTNGITPRRWIKQCNPALAALLDKSLQKEWAND
LDQLINLEKFADDAKFRQQYREIKQANKVRLAEFVKVRTGIEINPQAIFDIQIKRLHEYK
RQHLNLLHILALYKEIRENPQADRVPRVFLFGAKAAPGYYLAKNIIFAINKVADVINNDP
LVGDKLKVVFLPDYCVSAAEKLIPAADISEQISTAGKEASGTGNMKLALNGALTVGTLDG
ANVEIAEKVGEENIFIFGHTVEQVKAILAKGYDPVKWRKKDKVLDAVLKELESGKYSDGD
KHAFDQMLHSIGKQGGDPYLVMADFAAYVEAQKQVDVLYRDQEAWTRAAILNTARCGMFS
SDRSIRDYQARIWQAKR
References
External Links:
ResourceLink
Uniprot ID:P00490
Uniprot Name:PHSM_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676624
PDB ID:1QM5
Ecogene ID:EG10560
Ecocyc:EG10560
ColiBase:b3417
Kegg Gene:b3417
EchoBASE ID:EB0555
CCDB:PHSM_ECOLI
BacMap:49176351
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
  • Debarbouille, M., Cossart, P., Raibaud, O. (1982). "A DNA sequence containing the control sites for gene malT and for the malPQ operon." Mol Gen Genet 185:88-92. Pubmed: 6283313
  • 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
  • O'Reilly, M., Watson, K. A., Johnson, L. N. (1999). "The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex." Biochemistry 38:5337-5345. Pubmed: 10220320
  • Palm, D., Goerl, R., Burger, K. J. (1985). "Evolution of catalytic and regulatory sites in phosphorylases." Nature 313:500-502. Pubmed: 3155826
  • Palm, D., Goerl, R., Weidinger, G., Zeier, R., Fischer, B., Schinzel, R. (1987). "E. coli maltodextrin phosphorylase: primary structure and deletion mapping of the C-terminal site." Z Naturforsch C 42:394-400. Pubmed: 3037809
  • Pugsley, A. P., Dubreuil, C. (1988). "Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase." Mol Microbiol 2:473-479. Pubmed: 2845225
  • Raibaud, O., Debarbouille, M., Schwartz, M. (1983). "Use of deletions created in vitro to map transcriptional regulatory signals in the malA region of Escherichia coli." J Mol Biol 163:395-408. Pubmed: 6339728
  • Riley, M., Abe, T., Arnaud, M. B., Berlyn, M. K., Blattner, F. R., Chaudhuri, R. R., Glasner, J. D., Horiuchi, T., Keseler, I. M., Kosuge, T., Mori, H., Perna, N. T., Plunkett, G. 3rd, Rudd, K. E., Serres, M. H., Thomas, G. H., Thomson, N. R., Wishart, D., Wanner, B. L. (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34:1-9. Pubmed: 16397293
  • Schiltz, E., Palm, D., Klein, H. W. (1980). "N-terminal sequences of Escherichia coli and potato phosphorylase." FEBS Lett 109:59-62. Pubmed: 6986282
  • Watson, K. A., McCleverty, C., Geremia, S., Cottaz, S., Driguez, H., Johnson, L. N. (1999). "Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question." EMBO J 18:4619-4632. Pubmed: 10469642
  • Watson, K. A., Schinzel, R., Palm, D., Johnson, L. N. (1997). "The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase." EMBO J 16:1-14. Pubmed: 9009262
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842