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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   28-MAR-2018, entry version 146.
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.,
RA   Yamamoto Y., Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 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
RT   Salmonella typhimurium chromosomes and identification of two
RT   additional flagellar 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
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: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.
CC       {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.
CC       {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   ProteinModelPortal; P26612; -.
DR   SMR; P26612; -.
DR   BioGrid; 4260380; 11.
DR   DIP; DIP-9108N; -.
DR   IntAct; P26612; 4.
DR   STRING; 316385.ECDH10B_2068; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
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   EcoGene; EG11387; amyA.
DR   eggNOG; ENOG4105E5K; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   HOGENOM; HOG000094847; -.
DR   InParanoid; P26612; -.
DR   KO; K01176; -.
DR   OMA; VLNHKMG; -.
DR   PhylomeDB; P26612; -.
DR   BioCyc; EcoCyc:ALPHA-AMYL-CYTO-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; Complete proteome; Cytoplasm;
KW   Glycosidase; Hydrolase; Metal-binding; Reference proteome; Sodium.
FT   CHAIN         1    495       Cytoplasmic alpha-amylase.
FT                                /FTId=PRO_0000054287.
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     19     20       KL -> SS (in Ref. 1; AAA23810).
FT                                {ECO:0000305}.
FT   CONFLICT    109    109       A -> V (in Ref. 1; AAA23810).
FT                                {ECO:0000305}.
FT   CONFLICT    149    149       Q -> E (in Ref. 1; AAA23810).
FT                                {ECO:0000305}.
FT   CONFLICT    234    234       L -> I (in Ref. 1; AAA23810).
FT                                {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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