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Database: UniProt/SWISS-PROT
Entry: AMY2_SALTY
LinkDB: AMY2_SALTY
Original site: AMY2_SALTY 
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   28-FEB-2018, entry version 124.
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; Proteobacteria; 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.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   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
RT   Salmonella typhimurium chromosomes and identification of two
RT   additional flagellar 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
RT   non-coding region.";
RL   J. Gen. Microbiol. 139:1401-1407(1993).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {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.
CC       {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.
CC       {ECO:0000305}.
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   ProteinModelPortal; P26613; -.
DR   SMR; P26613; -.
DR   STRING; 99287.STM1963; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; P26613; -.
DR   EnsemblBacteria; AAL20875; AAL20875; STM1963.
DR   GeneID; 1253484; -.
DR   KEGG; stm:STM1963; -.
DR   PATRIC; fig|99287.12.peg.2079; -.
DR   eggNOG; ENOG4105E5K; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   HOGENOM; HOG000094847; -.
DR   KO; K01176; -.
DR   OMA; VLNHKMG; -.
DR   PhylomeDB; P26613; -.
DR   BioCyc; SENT99287:G1FZD-1981-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
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   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW   Glycosidase; Hydrolase; Metal-binding; Reference proteome; Sodium.
FT   CHAIN         1    494       Cytoplasmic alpha-amylase.
FT                                /FTId=PRO_0000054288.
FT   ACT_SITE    235    235       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    265    265       Proton donor. {ECO:0000250}.
FT   METAL       104    104       Calcium. {ECO:0000250|UniProtKB:P00692}.
FT   METAL       198    198       Calcium. {ECO:0000250|UniProtKB:P00692}.
FT   METAL       239    239       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00692}.
FT   SITE        332    332       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   CONFLICT    462    462       L -> S (in Ref. 1; AAA27110).
FT                                {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
//
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