ID   E0U1M0_BACSH            Unreviewed;       659 AA.
AC   E0U1M0;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 75.
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:ADM36368.1};
GN   OrderedLocusNames=BSUW23_01555 {ECO:0000313|EMBL:ADM36368.1};
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816 {ECO:0000313|EMBL:ADM36368.1, ECO:0000313|Proteomes:UP000002233};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W23;
RA   Zeigler D.R.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADM36368.1, ECO:0000313|Proteomes:UP000002233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23
RC   {ECO:0000313|Proteomes:UP000002233};
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
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; CP002183; ADM36368.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0U1M0; -.
DR   SMR; E0U1M0; -.
DR   CAZy; CBM26; Carbohydrate-Binding Module Family 26.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; bss:BSUW23_01555; -.
DR   HOGENOM; CLU_013336_4_1_9; -.
DR   Proteomes; UP000002233; 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..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..659
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038452544"
FT   DOMAIN          50..383
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          393..468
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   659 AA;  72431 MW;  504BD3983F9254F2 CRC64;
     MFEKRFKTSL LPLFAGFLLL FHLVLGGSAA ANAETQNTSK ELTAPSIKSG TILHAWNWSF
     NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGDKSMSNWY WLYQPTSYQI GNRYLGTEQE
     FKEMCAAAEE YGVKVIVDAV INHTTSDYAA ISNEIKSIPN WTHGNTQIKN WSDRWDVTQN
     SLLGLYDWNT QNAQVQSYLK RFLERALNDG ADGFRFDAAK HIELPDDGNY GSQFWPNITN
     TSAEFQYGEI LQDSASRDAA YANYMNVTAS NYGHSIRSAL KNRNLSVSNI SHYASDVSVD
     KLVTWVESHD TYANDEEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG GGNGVRFPGK
     SQIGDRGSGL FEDQAITAVN RFHNVMDGQP EELSNPNGNN QIFMNQRGSH GVVLANAGSS
     SVTINTSTKL PDGRYDNKAG NGSFQVTDGK LTGTLNARSV VVLYPDDIAN APHVFLENVK
     TGVTHSFNDQ LTITLRADAN TTKAVYQINN GQETAFKDGD QLTIGKGDSF GTTYNITLTG
     TNSDGVTRTQ EYRFVKKDPS AAKTIGYQNP NHWGQVNAYI YKHDGGRAIE LAGSWPGRAM
     AKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVQNGLYND SGLSGSLPH
//