ID   B7N219_ECO81            Unreviewed;       676 AA.
AC   B7N219;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CAR10390.2};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CAR10390.2};
GN   Name=malS {ECO:0000313|EMBL:CAR10390.2};
GN   OrderedLocusNames=ECED1_4259 {ECO:0000313|EMBL:CAR10390.2};
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR10390.2, ECO:0000313|Proteomes:UP000000748};
RN   [1] {ECO:0000313|Proteomes:UP000000748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR10390.2; -; Genomic_DNA.
DR   RefSeq; WP_000761207.1; NC_011745.1.
DR   AlphaFoldDB; B7N219; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ecq:ECED1_4259; -.
DR   HOGENOM; CLU_022115_1_0_6; -.
DR   Proteomes; UP000000748; 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:CAR10390.2};
KW   Hydrolase {ECO:0000313|EMBL:CAR10390.2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
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_5002857842"
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;  75759 MW;  13F0A99433D23F3A CRC64;
     MKLAACFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLM LNFDQQCWQP
     ADAIKLNQML SLQPCSNTPP QWRLFRDGEY TLQLDTRSGT PTLMISIQNA VEPVASLVRE
     CPKWDGLPLT LDVSATFAEG AAVRDYYSQQ IAIVKNGQIT LQPAATSNGL LLLERAETDT
     SAPFDWHNAT VYFVLTDRFE NGDPNNDQSY GRHKDGMAEI GTFHGGDLRG LTNKLDYLQQ
     LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGSK ADLRTLVDSA
     HQRGIRILFD VVMNHTGYAT LADMQEYQFG ALYLSGDELK KTLGERWSDW KPAAGQTWHS
     FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STSASGLPVF
     YKNKTDTHAK DIDGFTPRDY LTHWLSQWVR DYGIDGFRVD TAKHVELPAW QQLKTEASAA
     LREWKKANPD KALDDKPFWM TGEAWGHGVM QSDYYCYGFD AMINFDYQEQ AAKAVDCLAQ
     MDTTWQQMAE KLQDFNVLSY LSSHDTRLFR EGGDKAAELL LLAPGAVQIF YGDESSRPFG
     PTGSDPLQGT RSDMNWQDVS GKSAASVAHW QKISQFRARH PAIGAGKQTT LSLKQGYGFV
     REHGDDKVLV IWAGQQ
//