Beta-amylase

Name	Beta-amylase
Synonyms	1,4-alpha-D-glucan maltohydrolase 3.2.1.2
Gene Name	spoII
Organism	Bacillus cereus
Amino acid sequence	>lcl\|BSEQ0011327\|Beta-amylase MKNQFQYCCIVILSVVMLFVSLLIPQASSAAVNGKGMNPDYKAYLMAPLKKIPEVTNWET FENDLRWAKQNGFYAITVDFWWGDMEKNGDQQFDFSYAQRFAQSVKNAGMKMIPIISTHQ CGGNVGDDCNVPIPSWVWNQKSDDSLYFKSETGTVNKETLNPLASDVIRKEYGELYTAFA AAMKPYKDVIAKIYLSGGPAGELRYPSYTTSDGTGYPSRGKFQAYTEFAKSKFRLWVLNK YGSLNEVNKAWGTKLISELAILPPSDGEQFLMNGYLSMYGKDYLEWYQGILENHTKLIGE LAHNAFDTTFQVPIGAKIAGVHWQYNNPTIPHGAEKPAGYNDYSHLLDAFKSAKLDVTFT CLEMTDKGSYPEYSMPKTLVQNIATLANEKGIVLNGENALSIGNEEEYKRVAEMAFNYNF AGFTLLRYQDVMYNNSLMGKFKDLLGVTPVMQTIVVKNVPTTIGDTVYITGNRAELGSWD TKQYPIQLYYDSHSNDWRGNVVLPAERNIEFKAFIKSKDGTVKSWQTIQQSWNPVPLKTT SHTSSW
Number of residues	None
Molecular Weight	61628.585
Theoretical pI	6.72
GO Classification	Functions metal ion binding beta-amylase activity starch binding Processes polysaccharide catabolic process Components
General Function	Starch binding
Specific Function	None
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P36924
UniProtKB Entry Name
Cellular Location	Cytoplasmic
Gene sequence	>lcl\|BSEQ0003658\|1641 bp ATGAAAAATCAGTTTCAATATTGTTGTATTGTCATTTTGTCTGTAGTGATGTTATTTGTA TCATTATTAATTCCGCAAGCGAGTTCGGCAGCTGTAAATGGAAAAGGAATGAATCCAGAT TACAAAGCATATTTAATGGCGCCATTAAAAAAGATACCGGAAGTAACAAATTGGGAGACA TTTGAAAATGATTTACGATGGGCAAAACAAAATGGTTTTTATGCTATTACAGTTGATTTT TGGTGGGGGGATATGGAAAAGAACGGAGATCAGCAATTTGATTTTTCATACGCACAGCGC TTTGCTCAATCGGTAAAAAATGCAGGTATGAAAATGATTCCTATTATTTCCACACATCAG TGCGGTGGAAATGTTGGGGATGATTGCAATGTACCAATTCCTTCATGGGTTTGGAATCAA AAATCCGATGATAGCCTTTATTTTAAGTCTGAAACAGGAACTGTCAATAAAGAAACATTA AATCCACTTGCTTCAGATGTAATTCGAAAGGAATATGGTGAACTATATACAGCATTCGCA GCAGCTATGAAACCGTATAAAGATGTAATTGCAAAAATATATTTATCTGGAGGACCAGCT GGTGAACTAAGATATCCTTCATATACAACTTCCGATGGGACAGGATATCCCTCACGTGGA AAGTTTCAAGCGTATACAGAGTTTGCAAAATCTAAATTTCGTTTATGGGTATTAAATAAA TATGGTTCTCTAAATGAAGTGAATAAAGCATGGGGCACGAAACTGATTTCAGAGTTAGCA ATTTTACCACCAAGCGATGGGGAACAATTCTTAATGAATGGATATCTTTCTATGTATGGA AAAGACTATTTAGAATGGTATCAGGGCATCTTGGAAAATCATACAAAATTAATTGGTGAA TTAGCACATAACGCATTTGACACAACTTTCCAAGTACCAATTGGTGCAAAAATTGCAGGC GTACATTGGCAATATAATAACCCAACAATACCTCATGGAGCTGAAAAGCCTGCAGGGTAT AATGATTATAGCCATTTACTTGATGCTTTCAAAAGTGCAAAGCTAGATGTAACATTTACT TGCTTAGAAATGACAGATAAAGGTAGTTATCCGGAATATTCAATGCCAAAAACATTGGTA CAAAATATTGCAACATTAGCCAATGAAAAGGGAATTGTATTAAACGGTGAAAATGCTTTA AGTATCGGAAATGAAGAAGAGTATAAAAGAGTTGCAGAAATGGCTTTCAATTATAATTTT GCTGGATTTACGTTACTTCGTTATCAAGATGTAATGTATAACAATTCATTAATGGGGAAA TTTAAAGATTTATTAGGTGTAACCCCTGTTATGCAAACGATTGTAGTAAAAAATGTTCCT ACAACAATAGGAGATACTGTTTATATTACTGGGAATCGTGCGGAATTAGGAAGTTGGGAC ACAAAACAGTATCCAATTCAATTATATTATGATTCTCATAGTAATGATTGGAGAGGAAAT GTTGTGTTGCCAGCTGAAAGAAATATAGAATTTAAAGCATTTATTAAAAGTAAAGATGGA ACGGTTAAATCATGGCAAACAATACAACAAAGTTGGAATCCAGTGCCACTAAAGACTACC TCTCATACAAGTAGTTGGTAA
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Nanmori T, Nagai M, Shimizu Y, Shinke R, Mikami B: Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme. Appl Environ Microbiol. 1993 Feb;59(2):623-7. [8434930 ] Mikami B, Adachi M, Kage T, Sarikaya E, Nanmori T, Shinke R, Utsumi S: Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose. Biochemistry. 1999 Jun 1;38(22):7050-61. [10353816 ] Oyama T, Miyake H, Kusunoki M, Nitta Y: Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents. J Biochem. 2003 Apr;133(4):467-74. [12761294 ] Hirata A, Adachi M, Utsumi S, Mikami B: Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type. Biochemistry. 2004 Oct 5;43(39):12523-31. [15449941 ]

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