ID   Q7UAB0_SHIFL            Unreviewed;       495 AA.
AC   Q7UAB0;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=Cytoplasmic alpha-amylase {ECO:0000313|EMBL:AAP17349.1};
GN   Name=amyA {ECO:0000313|EMBL:AAP17349.1};
GN   OrderedLocusNames=S2066 {ECO:0000313|EMBL:AAP17349.1};
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623 {ECO:0000313|EMBL:AAP17349.1, ECO:0000313|Proteomes:UP000002673};
RN   [1] {ECO:0000313|EMBL:AAP17349.1, ECO:0000313|Proteomes:UP000002673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a
RC   {ECO:0000313|Proteomes:UP000002673};
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G.III., Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; AE014073; AAP17349.1; -; Genomic_DNA.
DR   RefSeq; WP_001245690.1; NZ_WPGW01000033.1.
DR   AlphaFoldDB; Q7UAB0; -.
DR   KEGG; sft:NCTC1_02142; -.
DR   KEGG; sfx:S2066; -.
DR   PATRIC; fig|623.158.peg.2171; -.
DR   HOGENOM; CLU_024572_2_0_6; -.
DR   OMA; CVVIMSN; -.
DR   Proteomes; UP000002673; 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   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;  56549 MW;  B223911C81CD834D CRC64;
     MRNPTLLQCF HWYYPEGGKL WPELAERADG FNDIGINMVW LPPAYKGASG GYSVGYDSYD
     LFDLGEFDQK GSIPTKYGDK AQLLAAIDAL KRNDIAVLLD VVVNHKMGAD EKEAIRVQRV
     NADDRTQIDE EIIECEGWTR YTFPARAGQY SQFIWDFKCF SGIDHIEHPD EDGIFKIVND
     YTGEGWNDQV DDELGNFDYL MGENIDFRNH AVTEEIKYWA RWVMEQTQCD GFRLDAVKHI
     PAWFYKEWIE HVQEVAPKPL FIVAECWSHE VDKLQTYIDQ VEGKTMLFDA PLQMKFHEAS
     RMGRDYDMTQ IFTGTLVEAD PFHAVTLVAN HDTQPLQALE APVEPWFKPL AYALILLREN
     GVPSVFYPDL YGAHYEDVGG DGQTYPIDMP IIEQLDELIL ARQRFAHGVQ TLFFDHPNCI
     AFSRSGTDEY PGCVVVMSNG DDGEKTIHLG ENYGNKTWRD FLGNRQESVV TDENGEATFF
     CNGGSVSVWV IEEVI
//