Maltogenic amylase

Name	Maltogenic amylase
Synonyms
Gene Name	None
Organism	Thermus sp. IM6501
Amino acid sequence	>lcl\|BSEQ0017024\|Maltogenic amylase MRKEAIHHRSTDNFAYAYDSETLHLRLQTKKNDVDHVELLFGDPYEWHDGAWQFQTMPMR KTGSDGLFDYWLAEVKPPYRRLRYGFVLRAGGEKLVYTEKGFYHEAPSDDTAYYFCFPFL HRVDLFQAPDWVKDTVWYQIFPERFANGNPAISPKGARPWGSEDPTPTSFFGGDLQGIID HLDYLADLGITGIYLTPIFRAPSNHKYDTADYFEIDPHFGDKETLKTLVKRCHEKGIRVM LDAVFNHCGYEFAPFQDVLKNGAASRYKDWFHIREFPLQTEPRPNYDTFAFVPHMPKLNT AHPEVKRYLLDVATYWIREFDIDGWRLDVANEIDHQFWREFRQAVKALKPDVYILGEIWH DAMPWLRGDQFDAVMNYPLADAALRFFAKEDMSASEFADRLMHVLHSYPKQVNEAAFNLL GSHDTPRLLTVCGGDVRKVKLLFLFQLTFTGSPCIYYGDEIGMTGGNDPECRKCMVWDPE KQNKELYEHVKQLIALRKQYRALRRGDVAFLTADDEVNHLVYAKTDGNETVMIIINRSNE AAEIPMPIDARGKWLVNLLTGERFAAEAETLCVSLPPYGFVLYAVESW
Number of residues	None
Molecular Weight	68209.815
Theoretical pI	5.86
GO Classification	Functions cation binding hydrolase activity, hydrolyzing O-glycosyl compounds Processes carbohydrate metabolic process Components
General Function	Hydrolase activity, hydrolyzing o-glycosyl compounds
Specific Function	None
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	O69007
UniProtKB Entry Name
Cellular Location	Cytoplasmic
Gene sequence	>lcl\|BSEQ0006247\|1767 bp ATGAGGAAAGAAGCCATCCACCACCGCTCAACCGACAATTTCGCTTATGCTTATGACAGC GAGACGCTCCATCTCCGGCTTCAAACAAAGAAAAATGATGTCGACCACGTCGAGCTGCTT TTTGGCGACCCGTACGAATGGCACGATGGCGCCTGGCAGTTTCAAACGATGCCGATGCGG AAAACGGGGAGCGACGGGTTGTTTGACTATTGGCTCGCCGAAGTCAAACCGCCATATCGA CGGCTGCGCTATGGGTTTGTGCTTCGAGCTGGGGGCGAGAAACTGGTCTATACGGAAAAA GGATTTTACCATGAAGCTCCGAGCGACGACACCGCTTACTACTTTTGCTTCCCCTTTCTT CATCGGGTCGACCTATTCCAAGCGCCGGACTGGGTAAAAGACACAGTATGGTATCAAATT TTCCCCGAGCGGTTCGCCAACGGCAACCCGGCCATCAGTCCGAAAGGGGCGCGGCCGTGG GGAAGCGAGGACCCGACGCCGACGAGCTTTTTCGGCGGCGACTTGCAAGGAATCATCGAT CACCTTGACTATTTGGCTGATCTCGGTATTACCGGCATTTACTTGACGCCGATTTTCCGC GCACCGTCCAATCATAAATACGACACCGCTGATTATTTTGAAATCGACCCGCACTTTGGG GACAAAGAGACGTTGAAAACACTTGTCAAGCGCTGCCATGAAAAAGGGATCCGCGTCATG CTCGATGCAGTCTTCAACCATTGCGGCTATGAGTTTGCCCCGTTTCAAGATGTGCTGAAA AACGGCGCAGCCTCTCGGTATAAAGATTGGTTCCATATTCGCGAGTTTCCGCTCCAAACC GAGCCGCGCCCGAACTACGACACGTTTGCGTTCGTGCCGCACATGCCGAAACTCAACACC GCTCATCCGGAAGTGAAGCGCTACTTGCTTGATGTCGCGACATACTGGATTCGCGAGTTT GATATTGACGGCTGGCGGCTCGATGTGGCGAACGAAATCGATCATCAATTTTGGCGCGAA TTCCGGCAGGCAGTGAAGGCGCTAAAGCCCGATGTGTACATTCTCGGCGAGATTTGGCAT GACGCCATGCCTTGGCTGCGCGGCGACCAGTTTGACGCCGTCATGAACTACCCGTTGGCG GACGCGGCGCTCCGCTTTTTCGCCAAAGAAGACATGAGCGCCAGCGAGTTTGCCGACCGA TTGATGCATGTGCTTCATTCCTATCCAAAACAGGTCAACGAAGCGGCGTTTAACTTGCTT GGCAGCCATGATACACCAAGGCTGCTCACTGTTTGCGGCGGCGACGTCCGCAAAGTGAAG TTGTTGTTTTTGTTCCAGCTCACGTTCACTGGTTCGCCGTGTATTTACTATGGCGATGAG ATCGGCATGACGGGTGGAAACGATCCGGAATGCCGGAAGTGTATGGTGTGGGATCCAGAG AAGCAAAACAAAGAACTGTATGAACATGTCAAGCAACTGATCGCTCTTCGCAAGCAATAT CGGGCGCTTCGACGCGGCGATGTCGCTTTTCTCACCGCCGATGATGAAGTGAACCATCTT GTTTATGCAAAAACGGATGGCAATGAAACGGTCATGATCATCATCAACCGGAGCAACGAA GCAGCAGAAATTCCCATGCCGATCGATGCGCGTGGAAAATGGCTGGTCAACCTTCTGACA GGGGAGCGGTTCGCTGCAGAGGCGGAAACACTTTGCGTCTCCTTGCCGCCGTACGGGTTT GTGCTTTACGCGGTCGAAAGCTGGTAA
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Kim TJ, Kim MJ, Kim BC, Kim JC, Cheong TK, Kim JW, Park KH: Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. Appl Environ Microbiol. 1999 Apr;65(4):1644-51. [10103262 ] Kim JS, Cha SS, Kim HJ, Kim TJ, Ha NC, Oh ST, Cho HS, Cho MJ, Kim MJ, Lee HS, Kim JW, Choi KY, Park KH, Oh BH: Crystal structure of a maltogenic amylase provides insights into a catalytic versatility. J Biol Chem. 1999 Sep 10;274(37):26279-86. [10473583 ] Lee HS, Kim MS, Cho HS, Kim JI, Kim TJ, Choi JH, Park C, Lee HS, Oh BH, Park KH: Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other. J Biol Chem. 2002 Jun 14;277(24):21891-7. Epub 2002 Mar 28. [11923309 ]

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