ID   Q8DPC8_STRR6            Unreviewed;       484 AA.
AC   Q8DPC8;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:AAL00043.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:AAL00043.1};
GN   Name=amy {ECO:0000313|EMBL:AAL00043.1};
GN   OrderedLocusNames=spr1239 {ECO:0000313|EMBL:AAL00043.1};
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101 {ECO:0000313|EMBL:AAL00043.1, ECO:0000313|Proteomes:UP000000586};
RN   [1] {ECO:0000313|EMBL:AAL00043.1, ECO:0000313|Proteomes:UP000000586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586};
RX   PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA   Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S.,
RA   DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., McHenney M.,
RA   McLeaster K., Mundy C., Nicas T.I., Norris F.H., O'Gara M., Peery R.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C., Baltz R.H., Jaskunas S.Richard.,
RA   Rosteck P.R.Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; AE007317; AAL00043.1; -; Genomic_DNA.
DR   PIR; F98026; F98026.
DR   RefSeq; NP_358832.1; NC_003098.1.
DR   RefSeq; WP_001181069.1; NC_003098.1.
DR   AlphaFoldDB; Q8DPC8; -.
DR   SMR; Q8DPC8; -.
DR   STRING; 171101.spr1239; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; spr:spr1239; -.
DR   PATRIC; fig|171101.6.peg.1345; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_024572_2_0_9; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
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; IPR006046; Alpha_amylase.
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   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:AAL00043.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAL00043.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000586}.
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   484 AA;  55880 MW;  DA511868187A0FFC CRC64;
     MQNQTLMQYF EWYLPHDGQH WTRLAENAPH LAHLGISHVW MPPAFKATNE KDVGYGVYDL
     FDLGEFNQKG TVRTKYGFKE DYLQAIQALK AQGIQPMADV VLNHKAAADH REAFQVIEVD
     PVDRTVELGE PFTINGWTSF TFDGRQDTYN GFHWHWYHFT GTDYDAKRSK SGIYLIQGDN
     KGWANEELVD NENGNYDYLM YADLDFKHPE VIQNIYDWAD WFMETTGVAG FRLDAVKHID
     SFFMRNFIRD MKEKYGDDFY VFGEFWNSDK EANLDYLEKT EEHFDLVDVR LHQNLFEASQ
     AGANYDLRGI FTDSLVELKP DKAVTFVDNH DTQRGQALES TVEEWFKPAA YALILLRQDG
     LPCVFYGDYY GISGQYAQQD FKEILDRLLA IRKDLAYGEQ NDYFDHANCI GWVRSGAENQ
     SPIAVLISND QENSKSMFVG QEWTNQTFVD LLGSHQGQVT IDEEGYGQFP VSARSVSVWA
     VNTI
//