ID   B5EX75_SALA4            Unreviewed;       675 AA.
AC   B5EX75;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:ACH51104.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:ACH51104.1};
GN   OrderedLocusNames=SeAg_B3878 {ECO:0000313|EMBL:ACH51104.1};
OS   Salmonella agona (strain SL483).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH51104.1, ECO:0000313|Proteomes:UP000008819};
RN   [1] {ECO:0000313|EMBL:ACH51104.1, ECO:0000313|Proteomes:UP000008819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483 {ECO:0000313|EMBL:ACH51104.1,
RC   ECO:0000313|Proteomes:UP000008819};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH51104.1; -; Genomic_DNA.
DR   RefSeq; WP_000761309.1; NC_011149.1.
DR   AlphaFoldDB; B5EX75; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; sea:SeAg_B3878; -.
DR   HOGENOM; CLU_022115_1_0_6; -.
DR   Proteomes; UP000008819; 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:ACH51104.1};
KW   Hydrolase {ECO:0000313|EMBL:ACH51104.1};
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..675
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002832963"
FT   DOMAIN          192..636
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        459
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   ACT_SITE        502
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   BINDING         313
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   SITE            564
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..536
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
SQ   SEQUENCE   675 AA;  75670 MW;  4DE2C2849403EF1D CRC64;
     MKLAAFALTL IPGIAIASSW TSPGFPTFST QETGRFTSHA ALTKGTRALT LHIDQQCWQP
     SGAIKLNQML SLKPCEGAPP QWRLFKDGDY TITVDTRSGT PTLLLSIKTE PERTAQLAYQ
     CPVWDGSPLT LDVRQTFPEG TVVRDYYSGQ TDTVQNGQIT LQPADSHGLL LLERAETHAS
     APFNWRNATV YFVLTDRFRN GDPTNDHSYG RHKDGMQEIG TFHGGDLRGL TSQLDYLQQL
     GVNALWISSP FEQIHGWVGG GTKGDFPHYA YHGYYTQDWT TLDANMGSEA DLRALVDGAH
     QRGIRILFDV VMNHAGYATL ADMQEYQFGA LYLSGAERQK ILGDRWTNWR PAAGQSWHSF
     NDYINFSDSA AWEKWWGKKW IRTDIGDYDS PGFDDLTLSL AFLPDIKTES TTPSGLPVFY
     ANKSDTKAKF IEGYTPRDYL THWLSQWVHD YGIDGFRVDT AKNVELPAWQ QLKTQASAAL
     HEWKQANPDK ALDNSPFWMT GEAWGHGVMK SDYYRYGFDA MINFDYQEQA AKAVDCLAEM
     GPVWQQMADK MQDFNVLSYL SSHDTRLFRE GGDKAAELLL LSPGAVQIFY GDESARPFGP
     TGSDPLQGTR SDMNWQDVSG KSAAAVAHWQ RISQFRARHP AIGAGQQTTL TLKHGYGFVR
     QYGDDTVMVV WAGRR
//