ID A0A1E5GK44_9ENTE Unreviewed; 494 AA.
AC A0A1E5GK44;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:OEG12965.1};
GN ORFNames=BCR25_05610 {ECO:0000313|EMBL:OEG12965.1};
OS Enterococcus termitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=332950 {ECO:0000313|EMBL:OEG12965.1, ECO:0000313|Proteomes:UP000095094};
RN [1] {ECO:0000313|EMBL:OEG12965.1, ECO:0000313|Proteomes:UP000095094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 8895 {ECO:0000313|EMBL:OEG12965.1,
RC ECO:0000313|Proteomes:UP000095094};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEG12965.1}.
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DR EMBL; MIJY01000023; OEG12965.1; -; Genomic_DNA.
DR RefSeq; WP_069663665.1; NZ_MIJY01000023.1.
DR AlphaFoldDB; A0A1E5GK44; -.
DR PATRIC; fig|332950.4.peg.2421; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000095094; Unassembled WGS sequence.
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..390
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 231
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 261
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 494 AA; 56551 MW; 9E19AFDBEAA4F36C CRC64;
MDNRTILQGF EWYLPADRRH WRRITEMAEK LHRLGINGVW LPPAYKGANG VNDVGYAPYD
LYDLGEFNQK GTISTKYGTK DEYLKCIKAL KNAGIDVYGD IVFDHFMGAD EEENVSAIKY
SPENRNERVS GEEEITAWTK FTFPGRKQIY NDYIWTWRNF SGIDFDDRRK DHGIFNFDGK
GWKEEVDQEN GNYDYLMGCN LDMANPETVE QLNKWGKWYQ ALTDLDGYRL DAVKHIQFNY
FVDWLLNRRN EKGKELFVVG EYWNGDVKKL INYIDRSGAL ISLFDVPLHY HLYEASSSNG
QYDMRNIFEE TLAKERPEWA VTFVDNHDTQ QGQSLESWVA GWFKVHAYAL ILLRKAGTPV
VFWGDLFGIP SQNVAPVGKD LPLLLKIRER LAYGNELDYF DDPSVVGWVR TGIFEKEKSG
YAVIMTNGAA GHKNMTVSAI HAGKTFVDIL GNNATKVILD EKGAGDFPVN GGEISVYVNE
GAVPSLTKNI EEFI
//
