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}.
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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
//