ID   D2AIB3_SHIF2            Unreviewed;       495 AA.
AC   D2AIB3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Cytoplasmic alpha-amylase {ECO:0000313|EMBL:ADA74352.1};
GN   Name=amyA {ECO:0000313|EMBL:ADA74352.1};
GN   OrderedLocusNames=SFxv_2199 {ECO:0000313|EMBL:ADA74352.1};
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020 {ECO:0000313|EMBL:ADA74352.1, ECO:0000313|Proteomes:UP000001884};
RN   [1] {ECO:0000313|EMBL:ADA74352.1, ECO:0000313|Proteomes:UP000001884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017 {ECO:0000313|EMBL:ADA74352.1,
RC   ECO:0000313|Proteomes:UP000001884};
RX   PubMed=19955273; DOI=10.1128/JCM.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(2010).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP001383; ADA74352.1; -; Genomic_DNA.
DR   RefSeq; WP_001245690.1; NC_017328.1.
DR   AlphaFoldDB; D2AIB3; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; sfe:SFxv_2199; -.
DR   PATRIC; fig|591020.3.peg.2379; -.
DR   HOGENOM; CLU_024572_2_0_6; -.
DR   Proteomes; UP000001884; 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; 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
//