Sequence of AMYB_BACCE
EC Number:3.2.1.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
Other sequences found for EC No. 3.2.1.2
General information:
Sequence
0 MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK KIPEVTNWET
60 FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR FAQSVKNAGM KMIPIISTHQ
120 CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS ETGTVNKETL NPLASDVIRK EYGELYTAFA
180 AAMKPYKDVI AKIYLSGGPA GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK
240 YGSLNEVNKA WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE
300 LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF KSAKLDVTFT
360 CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL SIGNEEEYKR VAEMAFNYNF
420 AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV MQTIVVKNVP TTIGDTVYIT GNRAELGSWD
480 TKQYPIQLYY DSHSNDWRGN VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT
540 SHTSSW
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
263770
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.
59
623-627
1993
263772
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
38
7050-7061
1999
263773
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.
133
467-474
2003
263774
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
43
12523-12531
2004