GenomeNet

Database: UniProt
Entry: C1C7Y2_STRP7
LinkDB: C1C7Y2_STRP7
Original site: C1C7Y2_STRP7 
ID   C1C7Y2_STRP7            Unreviewed;       484 AA.
AC   C1C7Y2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Alpha-amylase (1,4-alpha-D-glucanglucanohydrolase) {ECO:0000313|EMBL:ACO18012.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:ACO18012.1};
GN   OrderedLocusNames=SP70585_1420 {ECO:0000313|EMBL:ACO18012.1};
OS   Streptococcus pneumoniae (strain 70585).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488221 {ECO:0000313|EMBL:ACO18012.1, ECO:0000313|Proteomes:UP000002211};
RN   [1] {ECO:0000313|Proteomes:UP000002211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70585 {ECO:0000313|Proteomes:UP000002211};
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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}.
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; CP000918; ACO18012.1; -; Genomic_DNA.
DR   RefSeq; WP_001181074.1; NC_012468.1.
DR   AlphaFoldDB; C1C7Y2; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; snm:SP70585_1420; -.
DR   HOGENOM; CLU_024572_2_0_9; -.
DR   OMA; FFHWYYP; -.
DR   Proteomes; UP000002211; 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; 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:SF7; ALPHA-AMYLASE 2-RELATED; 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:ACO18012.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACO18012.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
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;  55953 MW;  111EF02212F1AF67 CRC64;
     MQNQTLMQYF EWYLPHDGQH WTRLAENAPH LAHLGISHVW MPPAFKATNE KDVGYGVYDL
     FDLGEFNQKG TVRTKYGFKE DYLQAIQALK EQGIQPMADV VLNHKAAADN REAFQVIEVD
     PVDRTVELGE PFTINGWTSF TFDGRQDTYN GFHWHWYHFT GTDYDAKRSK SGIYLIQGDN
     KGWANEELVD NENGNYDYLM YADLDFKHPE VIQNIYDWAD WFMETTGVAG FRLDAVKHID
     SFFMRNFIRD MKEKYGDDFY VFGEFWNPDK EANLDYLEKT EEHFDLVDVR LHQNLFEASQ
     AGANYDLRGI FTDSLVELKP DKAVTFVDNH DTQRGQALES TVEEWFKPAA YALILLRQDG
     LPCVFYGDYY GISGQYAQED FKEILDRLLA IRKDLAYGEQ NDYFDHANCI GWVRSGAENQ
     SPIAVLISND QENSKSMFVG QEWTNQTFVD LLGNHQGQVT IDEEGYGQFP VSARSVSVWA
     VNTI
//
DBGET integrated database retrieval system