ID   A7ZTB8_ECO24            Unreviewed;       676 AA.
AC   A7ZTB8;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Alpha-amylase, periplasmic {ECO:0000313|EMBL:ABV20110.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:ABV20110.1};
GN   Name=malS {ECO:0000313|EMBL:ABV20110.1};
GN   OrderedLocusNames=EcE24377A_4068 {ECO:0000313|EMBL:ABV20110.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV20110.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036917-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR036917-2};
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DR   EMBL; CP000800; ABV20110.1; -; Genomic_DNA.
DR   RefSeq; WP_000761263.1; NC_009801.1.
DR   AlphaFoldDB; A7ZTB8; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 66672540; -.
DR   KEGG; ecw:EcE24377A_4068; -.
DR   HOGENOM; CLU_022115_1_0_6; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030980; P:alpha-glucan catabolic process; IEA:InterPro.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR014635; A_amylase_MalS.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   PIRSF; PIRSF036917; Alph_amls_MalS; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR036917-2};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR036917-4};
KW   Glycosidase {ECO:0000313|EMBL:ABV20110.1};
KW   Hydrolase {ECO:0000313|EMBL:ABV20110.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001122};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..676
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002718857"
FT   DOMAIN          193..637
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        460
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   ACT_SITE        503
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   BINDING         314
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   BINDING         464
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   SITE            565
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-3"
FT   DISULFID        57..75
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
FT   DISULFID        121..537
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
SQ   SEQUENCE   676 AA;  75777 MW;  0736A575A7264431 CRC64;
     MKLAACFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP
     ADAIKLNQML SLQPCSNTPP QWRLFRDGKY TLQIDTRSGT PTLMISIQNA AEPVANLVRE
     CPKWDGLPLT LDVSATFPEG AAVRDYYSQQ IAIVKNGQIT LQPAATSNGL LLLERAETDA
     PAPFDWHNAT VYFVLTDRFE NGDPSNDQSY GRHKDGMAEI GTFHGGDLRG LTNKLDYLQQ
     LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGNE ADLRTLVDSA
     HQRGIRILFD VVMNHTGYAT LADMQEYQFG ALYLSGDEVK KTLGERWSDW KPAAGQTWHS
     FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STTASGLPVF
     YKNKTDTHAK VIEGFTPRDY LTHWLSQWVR DYGIDGFRVD TAKHVELPAW QQLKTEASAA
     LREWKKAYPD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ
     MDTTWQQMAE KLQGFNVLSY LSSHDTRLFR EGGDKAAELL LLAPGAVQIF YGDESSRPFG
     PTGSDPLQGT RSDMNWQDVS GKSAANVAHW QKISQFRARH PAIGAGKQTT LSLKQGYGFV
     REHGDDKVLV IWAGQQ
//