ID D3H1K3_ECO44 Unreviewed; 676 AA.
AC D3H1K3;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 13-SEP-2023, entry version 61.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CBG36700.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:CBG36700.1};
GN Name=malS {ECO:0000313|EMBL:CBG36700.1};
GN OrderedLocusNames=EC042_3877 {ECO:0000313|EMBL:CBG36700.1};
OS Escherichia coli O44:H18 (strain 042 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG36700.1, ECO:0000313|Proteomes:UP000001407};
RN [1] {ECO:0000313|EMBL:CBG36700.1, ECO:0000313|Proteomes:UP000001407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT "Complete genome sequence and comparative metabolic profiling of the
RT prototypical enteroaggregative Escherichia coli strain 042.";
RL PLoS ONE 5:E8801-E8801(2010).
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; FN554766; CBG36700.1; -; Genomic_DNA.
DR RefSeq; WP_000761246.1; NC_017626.1.
DR AlphaFoldDB; D3H1K3; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; elo:EC042_3877; -.
DR PATRIC; fig|216592.3.peg.4028; -.
DR HOGENOM; CLU_022115_1_0_6; -.
DR OMA; DKVMVVW; -.
DR Proteomes; UP000001407; 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; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF209; PERIPLASMIC ALPHA-AMYLASE; 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:CBG36700.1};
KW Hydrolase {ECO:0000313|EMBL:CBG36700.1};
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..676
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003044584"
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; 75768 MW; B37203F2AEF80DEA CRC64;
MKLAACFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP
ADAIKLNQML SLQPCSNTPP QWRLFRDGEY TLQLDTRSGT PTLMISIQNA VEPVASLVRE
CPKWDGLPLT LDVSATFPEG AAVRDYYSQQ IAIVKNGQIT LQPAATSNGL LLLERAETDT
SAPFDWHNAT VYFVLTDRFE NGDPSNDQSY GRHKDGMAEI GTFHGGDLRG LTNKLDYLQQ
LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGSE ADLRTLVDSA
HQRGIRILFD VVMNHTGYAT LADMQEYQFG ALYLSGDEVK KTLGERWSDW KPAAGQTWHS
FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STTASGLPVF
YKNKTDTHAK VIDGFTPRDY LTHWLSQWVR DYGIDGFRVD TVKHVELPAW QQLKTEASAA
LREWKKANPD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ
MDTTWQQMAE KLQDFNVLSY LSSHDTRLFR EGGDKAAELL LLAPGAVQIF YGDESSRPFG
PTGSDPLQGT RSDMNWQDVS GKSAASVAHW QKISQFRARH PAIGAGKQTT LSLKQGYGFV
REHGDDKVLV IWAGQQ
//