ID   AMY_THECU               Reviewed;         605 AA.
AC   P29750;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=tam;
OS   Thermomonospora curvata.
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Thermomonospora.
OX   NCBI_TaxID=2020;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCM 3352;
RX   PubMed=1551601; DOI=10.1016/0378-1119(92)90305-9;
RA   Petricek M., Tichy P., Kuncova M.;
RT   "Characterization of the alpha-amylase-encoding gene from Thermomonospora
RT   curvata.";
RL   Gene 112:77-83(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1756733; DOI=10.1002/j.1460-2075.1991.tb05004.x;
RA   Marcey D., Watkins W.S., Hazelrigg T.;
RT   "The temporal and spatial distribution pattern of maternal exuperantia
RT   protein: evidence for a role in establishment but not maintenance of bicoid
RT   mRNA localization.";
RL   EMBO J. 10:4259-4266(1991).
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;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 65 degrees Celsius.;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INDUCTION: By maltose or maltodextrins, even in the presence of
CC       glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X59159; CAA41881.1; -; Genomic_DNA.
DR   PIR; JH0638; JH0638.
DR   AlphaFoldDB; P29750; -.
DR   SMR; P29750; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
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   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW   Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..605
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001346"
FT   DOMAIN          500..605
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   ACT_SITE        219
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        253
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            313
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   605 AA;  64735 MW;  80ABB8F08A69B69A CRC64;
     MGVRRSLAAL LAALLGCATS LVALTVAASP AHAAPSGNRD VIVHLFQWRW KSIADECRTT
     LGPHGFGAVQ VSPPQEHVVL PAEDYPWWQD YQPVSYKLDQ TRRGSRADFI DMVNTCREAG
     VKIYVDAVIN HMTGTGSAGA GPGSAGSSYS KYDYPGIYQS QDFNDCRRDI TNWNDKWEVQ
     HCELVGLADL KTSSPYVQDR IAAYLNELID LGVAGFRIDA AKHIPEGDLQ AILSRLKNVH
     PAWGGGKPYI FQEVIADSTI STGSYTHLGS VTEFQYHRDI SHAFANGNIA HLTGLGSGLT
     PSDKAVVFVV NHDTQRYEPI LTHTDRARYD LAQKFMLAHP YGTPKVMSSY TWSGDDKAGP
     PMHSDGTTRP TDCSADRWLC EHRAVAGMVG FHNAVAGQGI GSAVTDGNGR LAFARGSAGY
     AAFNATNTAW TRTFTTSLPD GVYCDVANGT FVDGVCDGPS YQVSGGKFTA TVPANGAVAL
     HVEAPGSCGP DGCGTPPGGG DDCTTVTARF HATVTTWYGQ EVAVVGSIPE LGSWQPAQGV
     RLRTDSGTYP VWSGAVDLPA GVGFEYKYVK LNRTAPWSGS RAATASPPWM TSGGGCSQNF
     YDSWR