AMY1_ECOLI
ID AMY1_ECOLI Reviewed; 676 AA.
AC P25718; Q2M7N4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Periplasmic alpha-amylase;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=malS; OrderedLocusNames=b3571, JW3543;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 18-43.
RC STRAIN=K12;
RX PubMed=1544897; DOI=10.1016/s0021-9258(18)42743-3;
RA Schneider E., Freundlieb S., Tapio S., Boos W.;
RT "Molecular characterization of the MalT-dependent periplasmic alpha-amylase
RT of Escherichia coli encoded by malS.";
RL J. Biol. Chem. 267:5148-5154(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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 DISULFIDE BONDS.
RX PubMed=9268356; DOI=10.1074/jbc.272.35.22125;
RA Spiess C., Happersberger H.P., Glocker M.O., Spiess E., Rippe K.,
RA Ehrmann M.;
RT "Biochemical characterization and mass spectrometric disulfide bond mapping
RT of periplasmic alpha-amylase MalS of Escherichia coli.";
RL J. Biol. Chem. 272:22125-22133(1997).
CC -!- FUNCTION: Since only maltooligosaccharides up to a chain length of 6
CC glucose units are actively transported through the cytoplasmic membrane
CC via the membrane-bound complex of three proteins, MalF, MalG, and MalK,
CC longer maltooligosaccharides must first be degraded by the periplasmic
CC alpha-amylase, the MalS protein.
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;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Under the regulatory control of the MalT protein.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; X58994; CAA41740.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18548.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76595.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77722.1; -; Genomic_DNA.
DR PIR; S23807; S23807.
DR RefSeq; NP_418028.1; NC_000913.3.
DR RefSeq; WP_000761225.1; NZ_LN832404.1.
DR AlphaFoldDB; P25718; -.
DR SMR; P25718; -.
DR BioGRID; 4261712; 12.
DR DIP; DIP-10148N; -.
DR IntAct; P25718; 3.
DR STRING; 511145.b3571; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR jPOST; P25718; -.
DR PaxDb; P25718; -.
DR PRIDE; P25718; -.
DR EnsemblBacteria; AAC76595; AAC76595; b3571.
DR EnsemblBacteria; BAE77722; BAE77722; BAE77722.
DR GeneID; 948088; -.
DR KEGG; ecj:JW3543; -.
DR KEGG; eco:b3571; -.
DR PATRIC; fig|1411691.4.peg.3141; -.
DR EchoBASE; EB1292; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_022115_1_0_6; -.
DR InParanoid; P25718; -.
DR OMA; DKVMVVW; -.
DR PhylomeDB; P25718; -.
DR BioCyc; EcoCyc:ALPHA-AMYL-PERI-MON; -.
DR BioCyc; MetaCyc:ALPHA-AMYL-PERI-MON; -.
DR PRO; PR:P25718; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:EcoliWiki.
DR GO; GO:0005509; F:calcium ion binding; IDA:EcoCyc.
DR GO; GO:0030980; P:alpha-glucan catabolic process; IMP:EcoCyc.
DR GO; GO:0051692; P:cellular oligosaccharide catabolic process; IDA:EcoliWiki.
DR InterPro; IPR014635; A_amylase_MalS.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 2.
DR PIRSF; PIRSF036917; Alph_amls_MalS; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Metal-binding; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:1544897"
FT CHAIN 18..676
FT /note="Periplasmic alpha-amylase"
FT /id="PRO_0000001339"
FT ACT_SITE 460
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 503
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 565
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 57..75
FT /evidence="ECO:0000269|PubMed:9268356"
FT DISULFID 121..537
FT /evidence="ECO:0000269|PubMed:9268356"
SQ SEQUENCE 676 AA; 75713 MW; 980110EFA45E011D CRC64;
MKLAACFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP
ADAIKLNQML SLQPCSNTPP QWRLFRDGEY TLQIDTRSGT PTLMISIQNA AEPVASLVRE
CPKWDGLPLT VDVSATFPEG AAVRDYYSQQ IAIVKNGQIM LQPAATSNGL LLLERAETDT
SAPFDWHNAT VYFVLTDRFE NGDPSNDQSY GRHKDGMAEI GTFHGGDLRG LTNKLDYLQQ
LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGNE ADLRTLVDSA
HQRGIRILFD VVMNHTGYAT LADMQEYQFG ALYLSGDEVK KSLGERWSDW KPAAGQTWHS
FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STTASGLPVF
YKNKMDTHAK AIDGYTPRDY LTHWLSQWVR DYGIDGFRVD TAKHVELPAW QQLKTEASAA
LREWKKANPD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ
MDTTWQQMAE KLQGFNVLSY LSSHDTRLFR EGGDKAAELL LLAPGAVQIF YGDESSRPFG
PTGSDPLQGT RSDMNWQDVS GKSAASVAHW QKISQFRARH PAIGAGKQTT LLLKQGYGFV
REHGDDKVLV VWAGQQ
