ID   U5P4A4_9STRE            Unreviewed;       483 AA.
AC   U5P4A4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:AGY38468.1};
GN   ORFNames=N597_05785 {ECO:0000313|EMBL:AGY38468.1};
OS   Streptococcus ilei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY38468.1, ECO:0000313|Proteomes:UP000017124};
RN   [1] {ECO:0000313|EMBL:AGY38468.1, ECO:0000313|Proteomes:UP000017124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I-P16 {ECO:0000313|Proteomes:UP000017124};
RA   Hyun D.-W.;
RT   "Genome sequence of Streptococcus SP. I-P16 isolated from human ileal
RT   fluid.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP006776; AGY38468.1; -; Genomic_DNA.
DR   RefSeq; WP_023023735.1; NC_022582.1.
DR   AlphaFoldDB; U5P4A4; -.
DR   STRING; 1156433.N597_05785; -.
DR   KEGG; sip:N597_05785; -.
DR   PATRIC; fig|1156433.3.peg.1123; -.
DR   HOGENOM; CLU_024572_2_0_9; -.
DR   Proteomes; UP000017124; 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}.
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   483 AA;  55233 MW;  30B5B0C29C9C7638 CRC64;
     MENQTLMQYF EWYLPSDGQH WSRLAADAPH LADLGIRKIW MPPAFKATSA NDVGYGVYDL
     FDLGEFDQKG TVRTKYGFKE DYLQAIQALK EAGIQPMADV VLNHKAAADG LETFEVVEVD
     PNDRTIVLTE PFTIKGWTKF TFDGRNGAYN DFHWHWYHFT GTDYDASRNK SGIYQIQGEN
     KGWAQDYLVD SENGNYDYLM YADIDFKHPE VIENLNQWAE WFIETTGVQG FRLDAVKHID
     SFFMKNFIQQ ITDKYGEDFY VFGEFWNGDE QSNNDYLASI DYKFDLVDVA LHQNLFRASQ
     EGENFDLTTI FNGTLASNHP ESAVTFVDNH DTQRGQALES TVGEWFKPAA YALILLREAG
     LPCVFYGDYY GISGEFAQQD FQAELDQLLR IRKDLAYGEQ RDYFDDPNCI GWTRSGTEET
     APIACVISNA ASSAKRMEIG QVYAGQTYYD ALGNYQDTIQ IEEDGWADFP VSDRSVSVWV
     LAD
//