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 03-AUG-2022, entry version 137.
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., 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; P26613; -.
DR EnsemblBacteria; AAL20875; AAL20875; STM1963.
DR GeneID; 1253484; -.
DR KEGG; stm:STM1963; -.
DR PATRIC; fig|99287.12.peg.2079; -.
DR HOGENOM; CLU_024572_2_0_6; -.
DR OMA; FFHWYYP; -.
DR PhylomeDB; P26613; -.
DR BioCyc; SENT99287:STM1963-MON; -.
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: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; 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
