ID   B7LTI2_ESCF3            Unreviewed;       702 AA.
AC   B7LTI2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CAQ91041.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CAQ91041.1};
GN   Name=malS {ECO:0000313|EMBL:CAQ91041.1};
GN   OrderedLocusNames=EFER_3569 {ECO:0000313|EMBL:CAQ91041.1};
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ91041.1, ECO:0000313|Proteomes:UP000000745};
RN   [1] {ECO:0000313|Proteomes:UP000000745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC   JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC   {ECO:0000313|Proteomes:UP000000745};
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; CU928158; CAQ91041.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7LTI2; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; efe:EFER_3569; -.
DR   HOGENOM; CLU_022115_1_0_6; -.
DR   Proteomes; UP000000745; 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:CAQ91041.1};
KW   Hydrolase {ECO:0000313|EMBL:CAQ91041.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           44..702
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002857538"
FT   DOMAIN          219..663
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        486
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   ACT_SITE        529
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   BINDING         340
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   BINDING         490
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   SITE            591
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-3"
FT   DISULFID        83..101
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
FT   DISULFID        147..563
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
SQ   SEQUENCE   702 AA;  79300 MW;  A699916F4643D35B CRC64;
     MITREEFYRT YHWQTGEIRS NKSSSIMKLA ACFLLLLPGV AVAATWTSGG FPTFDEQSTG
     KYASHAQLTK GTRALTLNFD QQCWQPADAI KLNQMLSLKP CDSTPPQWRL FRDGEYTLQV
     DTRSGTPTLM ISVTSTAQPT INLIRECPKW DGQPLTLDVS QTFPEGAAIR EYYSQQIVTV
     KNGHITLKPV TESNGLLLLE HAETHTSAPF DWHNATVYFV LTDRFENGDP GNDQSYGRHK
     DGMQEIGTFH GGDLRGLTNK LDYLQQLGVN ALWISAPFEQ IHGWVGGGTK GDFPHYAYHG
     YYTQDWTNLD ANIGSEAELR ALVDGAHQRG IRIIFDVVMN HTGYATLADM QEFQFGALYL
     SGDELKKTLG ERWSDWKPAA GQTWHSFNDY INFSDKTGWE KWWGKNWIRT DIGDYDNPGF
     DDLTMSLAFL PDIKTESTTA SGLPVFYKNK PDTHAKAIDG YTPRDYLTHW LSQWVRDYGI
     DGFRVDTAKH VELPAWQQLK TEASAALNEW KKANPEKALD DNSFWMTGEA WGHGVMQSDY
     YRNGFDAMIN FDYQEQAAKA VDCLAQMDNI WQQMAEKLQD FNVLSYLSSH DTRLFREGGK
     KSAELLLLAP GAVQIFYGDE SLRPFGPTGS DPLQGTRSDM NWQDVSDKSA ASVKHWQRIS
     QFRARHLAIG AGKQTTLSLP QGYGFVREHG DDKVMVIWAG QH
//