ID   G4NTU0_BACS4            Unreviewed;       659 AA.
AC   G4NTU0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=GYO_0508 {ECO:0000313|EMBL:AEP85220.1};
OS   Bacillus spizizenii (strain DSM 15029 / JCM 12233 / NBRC 101239 / NRRL
OS   B-23049 / TU-B-10) (Bacillus subtilis subsp. spizizenii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1052585 {ECO:0000313|EMBL:AEP85220.1, ECO:0000313|Proteomes:UP000002651};
RN   [1] {ECO:0000313|EMBL:AEP85220.1, ECO:0000313|Proteomes:UP000002651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15029 / JCM 12233 / NBRC 101239 / NRRL B-23049 / TU-B-10
RC   {ECO:0000313|Proteomes:UP000002651};
RX   PubMed=22493193; DOI=10.1128/JB.05675-11;
RA   Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A.,
RA   Daugherty S., Losick R., Kolter R., Ravel J.;
RT   "Whole-genome sequences of Bacillus subtilis and close relatives.";
RL   J. Bacteriol. 194:2378-2379(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; CP002905; AEP85220.1; -; Genomic_DNA.
DR   RefSeq; WP_014112574.1; NC_016047.1.
DR   AlphaFoldDB; G4NTU0; -.
DR   STRING; 1052585.GYO_0508; -.
DR   KEGG; bst:GYO_0508; -.
DR   HOGENOM; CLU_013336_4_1_9; -.
DR   Proteomes; UP000002651; 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_5003466674"
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;  72476 MW;  D1C561D48F957FCC CRC64;
     MFEKRFKTSL LPLFAGFLLL FHLVLGGPAA ANAETQNTSN ELTAPSIKSG TILHAWNWSF
     NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGNKSMSNWY WLYQPTSYQI GNRYLGTEQE
     FKEMCAAAEE YGVKVIVDAV INHTTSDYAA ISNEIKSIPN WTHGNTQIKN WSDRWDVTQN
     SLLGLYDWNT QNTQVQSYLK RFLERALNDG ADGFRYDAAK HIELPDDGNY GSQFWPNITN
     TSAEFQYGEI LQDSASRDAA YANYMNVTAS NYGHSIRSAL KNRNLSVSNI SHYASEVSAD
     KLVTWVESHD TYANDEEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG GGNGVRFPGK
     SQIGDRGSAL FEDQAITAVN RFHNVMDGQP EELSNPNGNN QIFMNQRGSH GVVLANAGSS
     SVTINTSTKL PDGRYDNKAG NGSFQVTDGK LTGTINARSV AVLYSDDIAN APHVFLENVK
     TGVTHSFNDQ LTITLRADAN TTKAVYQINN GQETVFKDGD QLTIGKGDPF GTTYTITLTG
     TNSDGVTRTQ EYSFVKREPS AAKTIGYQNP NHWGQVNAYI YKHDGGRALE LTGSWPGKAM
     IKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVQNGLYND SGLSGSLPH
//