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 03-AUG-2022, entry version 162.
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}.
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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 AlphaFoldDB; P26612; -.
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 OMA; FFHWYYP; -.
DR PhylomeDB; P26612; -.
DR BioCyc; EcoCyc:ALPHA-AMYL-CYTO-MON; -.
DR BioCyc; MetaCyc:ALPHA-AMYL-CYTO-MON; -.
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: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 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 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