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Database: UniProt/SWISS-PROT
Entry: AMY1_ECOLI
LinkDB: AMY1_ECOLI
Original site: 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   27-SEP-2017, entry version 152.
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;
RA   Schneider E., Freundlieb S., Tapio S., Boos W.;
RT   "Molecular characterization of the MalT-dependent periplasmic alpha-
RT   amylase 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
RT   region 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.,
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   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
RT   mapping 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
CC       6 glucose units are actively transported through the cytoplasmic
CC       membrane via the membrane-bound complex of three proteins, MalF,
CC       MalG, and MalK, longer maltooligosaccharides must first be
CC       degraded by the periplasmic alpha-amylase, the MalS protein.
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.
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.
CC       {ECO:0000305}.
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   ProteinModelPortal; P25718; -.
DR   BioGrid; 4261712; 8.
DR   DIP; DIP-10148N; -.
DR   IntAct; P25718; 1.
DR   MINT; MINT-1293484; -.
DR   STRING; 316385.ECDH10B_3752; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
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   EcoGene; EG11316; malS.
DR   eggNOG; ENOG4107T9C; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   HOGENOM; HOG000273912; -.
DR   InParanoid; P25718; -.
DR   KO; K01176; -.
DR   PhylomeDB; P25718; -.
DR   BioCyc; EcoCyc:ALPHA-AMYL-PERI-MONOMER; -.
DR   BioCyc; MetaCyc:ALPHA-AMYL-PERI-MONOMER; -.
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:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
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; 1.
DR   PIRSF; PIRSF036917; Alph_amls_MalS; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 2.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Metal-binding; Periplasm; Reference proteome; Signal.
FT   SIGNAL        1     17       {ECO:0000269|PubMed:1544897}.
FT   CHAIN        18    676       Periplasmic alpha-amylase.
FT                                /FTId=PRO_0000001339.
FT   ACT_SITE    460    460       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    503    503       Proton donor. {ECO:0000250}.
FT   METAL       314    314       Calcium. {ECO:0000250}.
FT   METAL       464    464       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   SITE        565    565       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   DISULFID     57     75       {ECO:0000269|PubMed:9268356}.
FT   DISULFID    121    537       {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
//
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