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Database: UniProt/SWISS-PROT
Entry: AMY2_ECOLI
LinkDB: AMY2_ECOLI
Original site: AMY2_ECOLI 
ID   AMY2_ECOLI              Reviewed;         495 AA.
AC   P26612; P78072;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   12-AUG-2020, entry version 157.
DE   RecName: Full=Cytoplasmic alpha-amylase;
DE            EC=3.2.1.1 {ECO:0000269|PubMed:1400215};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
GN   Name=amyA; Synonyms=yedC; OrderedLocusNames=b1927, JW1912;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=JA11;
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=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RC   STRAIN=JA11;
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 475-495.
RC   STRAIN=JA11;
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:0000269|PubMed:1400215};
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1400215}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
DR   EMBL; L01642; AAA23810.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74994.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15755.1; -; Genomic_DNA.
DR   EMBL; M85240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L13279; AAA82575.1; -; Genomic_DNA.
DR   PIR; D64956; A45738.
DR   RefSeq; NP_416437.1; NC_000913.3.
DR   RefSeq; WP_001245695.1; NZ_LN832404.1.
DR   SMR; P26612; -.
DR   BioGRID; 4260380; 11.
DR   DIP; DIP-9108N; -.
DR   IntAct; P26612; 4.
DR   STRING; 511145.b1927; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   jPOST; P26612; -.
DR   PaxDb; P26612; -.
DR   PRIDE; P26612; -.
DR   EnsemblBacteria; AAC74994; AAC74994; b1927.
DR   EnsemblBacteria; BAA15755; BAA15755; BAA15755.
DR   GeneID; 946434; -.
DR   KEGG; ecj:JW1912; -.
DR   KEGG; eco:b1927; -.
DR   PATRIC; fig|1411691.4.peg.322; -.
DR   EchoBASE; EB1360; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_024572_2_0_6; -.
DR   InParanoid; P26612; -.
DR   KO; K01176; -.
DR   PhylomeDB; P26612; -.
DR   BioCyc; EcoCyc:ALPHA-AMYL-CYTO-MONOMER; -.
DR   BioCyc; ECOL316407:JW1912-MONOMER; -.
DR   BioCyc; MetaCyc:ALPHA-AMYL-CYTO-MONOMER; -.
DR   PRO; PR:P26612; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR   GO; GO:0004556; F:alpha-amylase activity; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW   Metal-binding; Reference proteome; Sodium.
FT   CHAIN           1..495
FT                   /note="Cytoplasmic alpha-amylase"
FT                   /id="PRO_0000054287"
FT   ACT_SITE        235
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   METAL           104
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250|UniProtKB:P00692"
FT   METAL           198
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250|UniProtKB:P00692"
FT   METAL           239
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P00692"
FT   SITE            332
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        19..20
FT                   /note="KL -> SS (in Ref. 1; AAA23810)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="A -> V (in Ref. 1; AAA23810)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="Q -> E (in Ref. 1; AAA23810)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="L -> I (in Ref. 1; AAA23810)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   495 AA;  56639 MW;  26AFF6797DDA54D6 CRC64;
     MRNPTLLQCF HWYYPEGGKL WPELAERADG FNDIGINMVW LPPAYKGASG GYSVGYDSYD
     LFDLGEFDQK GSIPTKYGDK AQLLAAIDAL KRNDIAVLLD VVVNHKMGAD EKEAIRVQRV
     NADDRTQIDE EIIECEGWTR YTFPARAGQY SQFIWDFKCF SGIDHIENPD EDGIFKIVND
     YTGEGWNDQV DDELGNFDYL MGENIDFRNH AVTEEIKYWA RWVMEQTQCD GFRLDAVKHI
     PAWFYKEWIE HVQEVAPKPL FIVAEYWSHE VDKLQTYIDQ VEGKTMLFDA PLQMKFHEAS
     RMGRDYDMTQ IFTGTLVEAD PFHAVTLVAN HDTQPLQALE APVEPWFKPL AYALILLREN
     GVPSVFYPDL YGAHYEDVGG DGQTYPIDMP IIEQLDELIL ARQRFAHGVQ TLFFDHPNCI
     AFSRSGTDEF PGCVVVMSNG DDGEKTIHLG ENYGNKTWRD FLGNRQERVV TDENGEATFF
     CNGGSVSVWV IEEVI
//
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