ID   AMY_BACSP               Reviewed;          20 AA.
AC   P86331;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Fragment;
OS   Bacillus sp.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1409;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Ferdowsicous;
RX   PubMed=20109486; DOI=10.1016/j.ijbiomac.2010.01.013;
RA   Asoodeh A., Chamani J., Lagzian M.;
RT   "A novel thermostable, acidophilic alpha-amylase from a new thermophilic
RT   'Bacillus sp. Ferdowsicous' isolated from Ferdows hot mineral spring in
RT   Iran: Purification and biochemical characterization.";
RL   Int. J. Biol. Macromol. 46:289-297(2010).
CC   -!- FUNCTION: Alpha-amylase active towards amylose, starch, amylopectin and
CC       maltodextrins. Has lower activity towards glycogen, and is not active
CC       towards alpha/beta-cyclodextrin. {ECO:0000269|PubMed:20109486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:20109486};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by Hg (2+). Inhibited by Zn
CC       (2+). Activated by Fe (2+), Mg (2+) and Ba (2+).
CC       {ECO:0000269|PubMed:20109486}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.5. Stable from pH 4.0-7.5, activity decreases
CC         drastically above pH 7.5 and below pH 3.5.
CC         {ECO:0000269|PubMed:20109486};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius. Active from 30 to 75
CC         degrees Celsius, inactivated following 150 minutes incubation at 85
CC         degrees Celsius. {ECO:0000269|PubMed:20109486};
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DR   AlphaFoldDB; P86331; -.
DR   BRENDA; 3.2.1.1; 16643.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase.
FT   CHAIN           1..>20
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000383667"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2516 MW;  752898C5A060BF77 CRC64;
     AHQLPMGTLC NFYEWYRRDD