ID   I2C144_BACAY            Unreviewed;       662 AA.
AC   I2C144;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=amyE {ECO:0000313|EMBL:AFJ60368.1};
GN   ORFNames=MUS_0286 {ECO:0000313|EMBL:AFJ60368.1};
OS   Bacillus amyloliquefaciens (strain Y2) (Bacillus amyloliquefaciens subsp.
OS   plantarum (strain B9601-Y2)).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1155777 {ECO:0000313|EMBL:AFJ60368.1, ECO:0000313|Proteomes:UP000002878};
RN   [1] {ECO:0000313|EMBL:AFJ60368.1, ECO:0000313|Proteomes:UP000002878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y2 {ECO:0000313|EMBL:AFJ60368.1};
RX   PubMed=23357245; DOI=10.1016/j.jbiotec.2012.12.014;
RA   He P., Hao K., Blom J., Ruckert C., Vater J., Mao Z., Wu Y., Hou M., He P.,
RA   He Y., Borriss R.;
RT   "Genome sequence of the plant growth promoting strain Bacillus
RT   amyloliquefaciens subsp. plantarum B9601-Y2 and expression of mersacidin
RT   and other secondary metabolites.";
RL   J. Biotechnol. 164:281-291(2012).
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:0000256|ARBA:ARBA00000548,
CC         ECO:0000256|RuleBase:RU361134};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP003332; AFJ60368.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2C144; -.
DR   SMR; I2C144; -.
DR   KEGG; bqy:MUS_0286; -.
DR   PATRIC; fig|1126211.3.peg.277; -.
DR   HOGENOM; CLU_013336_4_1_9; -.
DR   Proteomes; UP000002878; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11315; AmyAc_bac1_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR031965; CBM26.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF16738; CBM26; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..662
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038813107"
FT   DOMAIN          53..386
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          396..471
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   662 AA;  72689 MW;  EEA28DB236C3FC8D CRC64;
     MSKMFKKRFK TSLLPLFAGF LLLFHLVLSG PAAANAETAH KSNEVTDSSV KNGTILHAWN
     WSFNTLTENM KEIRDAGYAA IQTSPINQVK EGNQGDKSMS NWYWLYQPTS YQIGNRYLGT
     EQEFKDMCAA AEKYGVKVIV DAVVNHTTSD YGAISDEIKR IPNWTHGNTQ IKNWSDRWDI
     TQNALLGLYD WNTQNTEVQA YLKGFLERAL NDGADGFRYD AAKHIELPDD GNYGSQFWPN
     ITNTSAEFQY GEILQDSASR DTAYANYMNV TASNYGHSIR SALKNRNLSV SNISHYASDV
     SADKLVTWVE SHDTYANDDE ESTWMSDDDI RLGWAVIGSR SGSTPLFFSR PEGGGNGVRF
     PGKSQIGDRG SALFKDQAIT AVNQFHNEMA GQPEELSNPN GNNQIFMNQR GSKGVVLANA
     GSSSVTINTS TKLPDGRYDN RAGAGSFQVA NGKLTGTINA RSAAVLYPDD IGNAPHVFLE
     NYQTEAVHSF NDQLTVTLRA NAKTAKAVYQ INNGQETAFK DGDRLTIGKE DPIGTTYNVK
     LTGTNGEGAS RTQEYTFVKK DPSQTNIIGY QNPDHWGQVN AYIYKHDGGG AIELTGSWPG
     KAMTKNADGI YTLTLPANAD TADAKVIFNN GSAQVPGQNQ PGFDYVQNGL YNNSGLNGYL
     TH
//