ID   AMY2_SALTY              Reviewed;         494 AA.
AC   P26613;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 3.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Cytoplasmic alpha-amylase;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P06279};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
GN   Name=amyA; OrderedLocusNames=STM1963;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SJW1103;
RX   PubMed=1400215; DOI=10.1128/jb.174.20.6644-6652.1992;
RA   Raha M., Kawagishi I., Mueller V., Kihara M., Macnab R.M.;
RT   "Escherichia coli produces a cytoplasmic alpha-amylase, AmyA.";
RL   J. Bacteriol. 174:6644-6652(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC   STRAIN=SJW1103;
RX   PubMed=1527488; DOI=10.1099/00221287-138-6-1051;
RA   Kawagishi I., Mueller V., Williams A.W., Irikura V.M., Macnab R.M.;
RT   "Subdivision of flagellar region III of the Escherichia coli and Salmonella
RT   typhimurium chromosomes and identification of two additional flagellar
RT   genes.";
RL   J. Gen. Microbiol. 138:1051-1065(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 476-494.
RX   PubMed=8371104; DOI=10.1099/00221287-139-7-1401;
RA   Raha M., Kihara M., Kawagishi I., Macnab R.M.;
RT   "Organization of the Escherichia coli and Salmonella typhimurium
RT   chromosomes between flagellar regions IIIa and IIIb, including a large non-
RT   coding region.";
RL   J. Gen. Microbiol. 139:1401-1407(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P06279};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P06278};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P06278};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P26612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26612}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; L01643; AAA27110.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20875.1; -; Genomic_DNA.
DR   EMBL; M85241; AAA27079.1; -; Genomic_DNA.
DR   EMBL; L13280; AAA71970.1; -; Unassigned_DNA.
DR   PIR; B45738; B45738.
DR   RefSeq; NP_460916.1; NC_003197.2.
DR   RefSeq; WP_000795487.1; NC_003197.2.
DR   AlphaFoldDB; P26613; -.
DR   SMR; P26613; -.
DR   STRING; 99287.STM1963; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 99287-STM1963; -.
DR   GeneID; 1253484; -.
DR   KEGG; stm:STM1963; -.
DR   PATRIC; fig|99287.12.peg.2079; -.
DR   HOGENOM; CLU_024572_2_0_6; -.
DR   OMA; CVVIMSN; -.
DR   PhylomeDB; P26613; -.
DR   BioCyc; SENT99287:STM1963-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW   Metal-binding; Reference proteome; Sodium.
FT   CHAIN           1..494
FT                   /note="Cytoplasmic alpha-amylase"
FT                   /id="PRO_0000054288"
FT   ACT_SITE        235
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00692"
FT   BINDING         198
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00692"
FT   BINDING         239
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00692"
FT   SITE            332
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        462
FT                   /note="L -> S (in Ref. 1; AAA27110)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  56522 MW;  5C1E862FEDD5E47C CRC64;
     MKNPTLLQYF HWYYPDGGKL WSELAERADG LNDIGINMVW LPPACKGASG GYSVGYDTYD
     LFDLGEFDQK GTIATKYGDK RQLLTAIDAL KKNNIAVLLD VVVNHKMGAD EKERIRVQRV
     NQDDRTQIDD NIIECEGWTR YTFPARAGQY SNFIWDYHCF SGIDHIENPD EDGIFKIVND
     YTGDGWNDQV DDEMGNFDYL MGENIDFRNH AVTEEIKYWA RWVMEQTHCD GFRLDAVKHI
     PAWFYKEWIE HVQAVAPKPL FIVAEYWSHE VDKLQTYIDQ VDGKTMLFDA PLQMKFHEAS
     RQGAEYDMRH IFTGTLVEAD PFHAVTLVAN HDTQPLQALE APVEPWFKPL AYALILLREN
     GVPSVFYPDL YGASYEDSGE NGETCRVDMP VINQLDRLIL ARQRFAHGIQ TLFFDHPNCI
     AFSRSGTEEN PGCVVVLSNG DDGEKTLLLG DNYANKTWRD FLGNRDEYVV TNDQGEATFF
     CNAGSVSVWV IEDV
//