ID   Q5M393_STRT2            Unreviewed;       491 AA.
AC   Q5M393;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:AAV61145.1};
GN   Name=amyL {ECO:0000313|EMBL:AAV61145.1};
GN   OrderedLocusNames=stu1542 {ECO:0000313|EMBL:AAV61145.1};
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV61145.1, ECO:0000313|Proteomes:UP000001170};
RN   [1] {ECO:0000313|EMBL:AAV61145.1, ECO:0000313|Proteomes:UP000001170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170};
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP000023; AAV61145.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5M393; -.
DR   STRING; 264199.stu1542; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; stl:stu1542; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_024572_2_0_9; -.
DR   Proteomes; UP000001170; Chromosome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR   Gene3D; 2.40.30.140; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013776; A-amylase_thermo.
DR   InterPro; IPR015237; Alpha-amylase_C_pro.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF09154; Alpha-amy_C_pro; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001170}.
FT   DOMAIN          12..400
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        242
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   491 AA;  57031 MW;  6B4075225CBF4E64 CRC64;
     MSTNKEKTMT NQTAMQYFEW YLPSDGQHWN NLAEDAQHLA DLGISHVWMP PAFKATNKDD
     VGYGVYDLFD LGEFDQKGTI RTKYGLKEEY LNAINQLKNV GIIPMADVVL NHKAAADKLE
     TFYVVEVDPE DRTKVISEPF EIEGWTHFTF DGRQKAYNDF EWHWYHFNGT DFDAKRNKKG
     IYLIQGDNKG WAHNDLVDNE NGNFDYLMFA NLDYRHPEVI ENIYEWADWF VETTGVQGFR
     MDAIKHIDYF FMRNFIRDVK EKQGQDFYVF GEFWNAKEED NNTYLEKTEN RFDLVDVRLH
     YNLYDASLKG ADYDLTTIFE QTLVKNHPEH AVTFVENHDT QRGQALESTV EEWFKPSAYA
     LILLRKDGLP CLFYGDYYGI DGEFAQESFK EVLDTLLYAR KDLAYGEQTD YFDDPNCIGW
     TRSGNEDCTP LAVTISNDAA NNKSMEIGSD WAGQTFYDIL GNCSDTVTID EDGWGDFPVS
     EKSVSVWTIQ D
//