ID   B7LP38_ESCF3            Unreviewed;       495 AA.
AC   B7LP38;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Cytoplasmic alpha-amylase {ECO:0000313|EMBL:CAQ88694.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CAQ88694.1};
GN   Name=amyA {ECO:0000313|EMBL:CAQ88694.1};
GN   OrderedLocusNames=EFER_1166 {ECO:0000313|EMBL:CAQ88694.1};
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ88694.1, ECO:0000313|Proteomes:UP000000745};
RN   [1] {ECO:0000313|Proteomes:UP000000745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC   JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC   {ECO:0000313|Proteomes:UP000000745};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CU928158; CAQ88694.1; -; Genomic_DNA.
DR   RefSeq; WP_000795463.1; NC_011740.1.
DR   AlphaFoldDB; B7LP38; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 75057787; -.
DR   KEGG; efe:EFER_1166; -.
DR   HOGENOM; CLU_024572_2_0_6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000000745; 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:CAQ88694.1};
KW   Hydrolase {ECO:0000313|EMBL:CAQ88694.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
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   495 AA;  56453 MW;  C44BE13501FF2A4F CRC64;
     MKNPTLLQCF HWYYPEGGQL WPELAERADG LNDIGINMVW LPPAYKGASG GYSVGYDSYD
     LFDLGEFDQK GTIPTKYGDK AQLLGAIDAL KRNNIAVLLD VVVNHKMGAD EKEAIRVQRV
     NEDDRTQIDD EIIECEGWTR YTFPARAGKY SQFIWDFKCF SGIDHIENPN EDGIFKIVND
     YTGEGWNDQV DDELGNFDYL MGENIDFRNH AVTEEIKYWA RWVMEQTQCD GFRLDAVKHI
     PAWFYKEWIE HVQEVAPKPL FIVAEYWSHE VDKLQTYIDQ VEGKTMLFDA PLQMKFHEAS
     RMGRDYDMTQ IFTGTLVEAD PFHAVTLVAN HDTQPLQALE APVEPWFKPL AYALILLREN
     GVPSVFYPDL YGAHYEDVGG DGQTYPINMP VIEQLDELIL ARQRFAHGVQ TLYFDHPNCI
     AFSRSGTDEA PGCVVIMSNG DDGEKTITLG ENYGNKTWRD FLGNRQESVV TDENGEATFF
     CNGGSVSVWV IEEVI
//