ID   Q8DT08_STRMU            Unreviewed;       486 AA.
AC   Q8DT08;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Intracellular alpha-amylase {ECO:0000313|EMBL:AAN59233.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:AAN59233.1};
GN   Name=amyA {ECO:0000313|EMBL:AAN59233.1};
GN   OrderedLocusNames=SMU_1590 {ECO:0000313|EMBL:AAN59233.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59233.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN59233.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014133; AAN59233.1; -; Genomic_DNA.
DR   RefSeq; NP_721927.1; NC_004350.2.
DR   RefSeq; WP_002263876.1; NC_004350.2.
DR   AlphaFoldDB; Q8DT08; -.
DR   STRING; 210007.SMU_1590; -.
DR   KEGG; smu:SMU_1590; -.
DR   PATRIC; fig|210007.7.peg.1415; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_024572_2_0_9; -.
DR   OrthoDB; 9805159at2; -.
DR   PhylomeDB; Q8DT08; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; 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   Glycosidase {ECO:0000313|EMBL:AAN59233.1};
KW   Hydrolase {ECO:0000313|EMBL:AAN59233.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT   DOMAIN          4..392
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        264
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         197
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         203
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="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         238
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   486 AA;  56458 MW;  EF482B92FB37C4D8 CRC64;
     MTNETMMQYF EWYLPNDGKH WQHLAEDASH LKNIGISKVW MPPAFKGTGS NDVGYGVYDL
     YDLGEFNQNG TVRTKYGSRE DYLNAVNALK EQEIMPISDI VLNHKANGDA KERFQVVKVN
     PSNRQEKISE PYEIEGWTQF NFPGRQDNYS DFKWHWYHFT GVDYDALHNE NGIYMILGDN
     KGWASQENID QENGNYDYLM YDDIDFKHPE VQEHLRDWVA WFLETSGVGG FRLDAIKHID
     KTFMAQFIRY IREHLKADLY VFGEYWKDSH FDITDYLHSV DLQFDLIDVM LHMSLFEAGQ
     KGSDFDLSTI LDDSLMKSHP DFAVTFVDNH DSQRGQALES TVAEWFKPLA YGLILLRQEG
     IPCVFYGDYY GISGEFAQES FQTVLDKLLY IRQYHVYGSQ EDYFDYANCI GWTCLGDEEH
     PDGVAVIISN GEANCKRMNM GEFNRNKVFV DYLNNCTEEV ILDDQGWGDF PVQEASLSAW
     VNKDAH
//