ID   D8MTL6_ERWBE            Unreviewed;       493 AA.
AC   D8MTL6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Cytoplasmic alpha-amylase {ECO:0000313|EMBL:CAX60173.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CAX60173.1};
GN   Name=amyA {ECO:0000313|EMBL:CAX60173.1};
GN   OrderedLocusNames=EbC_26420 {ECO:0000313|EMBL:CAX60173.1};
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN   [1] {ECO:0000313|EMBL:CAX60173.1, ECO:0000313|Proteomes:UP000008793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661 {ECO:0000313|EMBL:CAX60173.1,
RC   ECO:0000313|Proteomes:UP000008793};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; FP236843; CAX60173.1; -; Genomic_DNA.
DR   RefSeq; WP_013202659.1; NC_014306.1.
DR   AlphaFoldDB; D8MTL6; -.
DR   STRING; 634500.EbC_26420; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ebi:EbC_26420; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_024572_2_0_6; -.
DR   Proteomes; UP000008793; 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; 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; 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   Glycosidase {ECO:0000313|EMBL:CAX60173.1};
KW   Hydrolase {ECO:0000313|EMBL:CAX60173.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT   DOMAIN          4..402
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        235
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        265
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         198
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         206
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         239
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   493 AA;  56237 MW;  60BFC389DF049500 CRC64;
     MPNSTLLQFF HWYYPDGSKL WPEAAERAEK LAEIGITDVW LPPAYKGESG GYSVGYDSYD
     LFDLGEFDQK GSRATKYGDK EQLKAAVDAL RAHQVGVIMD VVLNHKMGAD EKERIQVNRT
     NPDNRDEIDP VAFEADAWTK FTFPVRAGQY SKFVWDYKCF NGVDYIENPD ENGVFKIVND
     YTGEGWNDQV DDELGNFDYL MGANIDFRNH AVTEELKYWA RWMLEQLPCT GFRLDAVKHI
     PAWFYKEWIE HVQEVAEQPL FIVAEYWSHE VDKLQQYIHQ VEGKTMLFDA PLQMKFHNAS
     REGASYDLSQ IFNDTLVEKD HWHAVTIVAN HDTQPLQSLE APVEPWFKPL AYALILLREQ
     GVPVVFYPDL FGASYEDEGG DGENHHIDMP VIPELEALIR ARQLYAHGVQ TEWFNHPNCV
     AFARSGTEEQ PGCVVILSNG DAGEKTLPMG EALAGKSWRD YLGHQTETIT ADDKGNTVFR
     CNPGSVSVWV LTE
//