Maltodextrin phosphorylase

Name	Maltodextrin phosphorylase
Synonyms	2.4.1.1
Gene Name	malP
Organism	Escherichia coli (strain K12)
Amino acid sequence	>lcl\|BSEQ0016526\|Maltodextrin phosphorylase MSQPIFNDKQFQEALSRQWQRYGLNSAAEMTPRQWWLAVSEALAEMLRAQPFAKPVANQR HVNYISMEFLIGRLTGNNLLNLGWYQDVQDSLKAYDINLTDLLEEEIDPALGNGGLGRLA ACFLDSMATVGQSATGYGLNYQYGLFRQSFVDGKQVEAPDDWHRSNYPWFRHNEALDVQV GIGGKVTKDGRWEPEFTITGQAWDLPVVGYRNGVAQPLRLWQATHAHPFDLTKFNDGDFL RAEQQGINAEKLTKVLYPNDNHTAGKKLRLMQQYFQCACSVADILRRHHLAGRKLHELAD YEVIQLNDTHPTIAIPELLRVLIDEHQMSWDDAWAITSKTFAYTNHTLMPEALERWDVKL VKGLLPRHMQIINEINTRFKTLVEKTWPGDEKVWAKLAVVHDKQVHMANLCVVGGFAVNG VAALHSDLVVKDLFPEYHQLWPNKFHNVTNGITPRRWIKQCNPALAALLDKSLQKEWAND LDQLINLEKFADDAKFRQQYREIKQANKVRLAEFVKVRTGIEINPQAIFDIQIKRLHEYK RQHLNLLHILALYKEIRENPQADRVPRVFLFGAKAAPGYYLAKNIIFAINKVADVINNDP LVGDKLKVVFLPDYCVSAAEKLIPAADISEQISTAGKEASGTGNMKLALNGALTVGTLDG ANVEIAEKVGEENIFIFGHTVEQVKAILAKGYDPVKWRKKDKVLDAVLKELESGKYSDGD KHAFDQMLHSIGKQGGDPYLVMADFAAYVEAQKQVDVLYRDQEAWTRAAILNTARCGMFS SDRSIRDYQARIWQAKR
Number of residues	None
Molecular Weight	90521.74
Theoretical pI	7.41
GO Classification	Functions pyridoxal phosphate binding glycogen phosphorylase activity maltodextrin phosphorylase activity Processes glycogen catabolic process alpha-glucan catabolic process Components cytoplasm cytosol
General Function	Pyridoxal phosphate binding
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.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P00490
UniProtKB Entry Name
Cellular Location	None
Gene sequence	>lcl\|BSEQ0016527\|Maltodextrin phosphorylase (malP) 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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Palm D, Goerl R, Weidinger G, Zeier R, Fischer B, Schinzel R: E. coli maltodextrin phosphorylase: primary structure and deletion mapping of the C-terminal site. Z Naturforsch C. 1987 Apr;42(4):394-400. [3037809 ] Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [9278503 ] Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G 3rd, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL: Escherichia coli K-12: a cooperatively developed annotation snapshot--2005. Nucleic Acids Res. 2006 Jan 5;34(1):1-9. Print 2006. [16397293 ] Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [16738553 ] Palm D, Goerl R, Burger KJ: Evolution of catalytic and regulatory sites in phosphorylases. Nature. 1985 Feb 7-13;313(6002):500-2. [3155826 ] Pugsley AP, Dubreuil C: Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase. Mol Microbiol. 1988 Jul;2(4):473-9. [2845225 ] Debarbouille M, Cossart P, Raibaud O: A DNA sequence containing the control sites for gene malT and for the malPQ operon. Mol Gen Genet. 1982;185(1):88-92. [6283313 ] Raibaud O, Debarbouille M, Schwartz M: Use of deletions created in vitro to map transcriptional regulatory signals in the malA region of Escherichia coli. J Mol Biol. 1983 Jan 25;163(3):395-408. [6339728 ] Schiltz E, Palm D, Klein HW: N-terminal sequences of Escherichia coli and potato phosphorylase. FEBS Lett. 1980 Jan 1;109(1):59-62. [6986282 ] Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [18723842 ] Watson KA, Schinzel R, Palm D, Johnson LN: 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. 1997 Jan 2;16(1):1-14. [9009262 ] O'Reilly M, Watson KA, Johnson LN: The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex. Biochemistry. 1999 Apr 27;38(17):5337-45. [10220320 ] Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H, Johnson LN: Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question. EMBO J. 1999 Sep 1;18(17):4619-32. [10469642 ]

From www.t3db.ca