ID B7ULD2_ECO27 Unreviewed; 676 AA.
AC B7ULD2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CAS11371.1};
GN Name=malS {ECO:0000313|EMBL:CAS11371.1};
GN OrderedLocusNames=E2348C_3823 {ECO:0000313|EMBL:CAS11371.1};
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS11371.1, ECO:0000313|Proteomes:UP000008205};
RN [1] {ECO:0000313|EMBL:CAS11371.1, ECO:0000313|Proteomes:UP000008205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX PubMed=18952797; DOI=10.1128/JB.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(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; FM180568; CAS11371.1; -; Genomic_DNA.
DR RefSeq; WP_000762038.1; NC_011601.1.
DR AlphaFoldDB; B7ULD2; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; ecg:E2348C_3823; -.
DR HOGENOM; CLU_022115_1_0_6; -.
DR OMA; DKVMVVW; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008205};
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_5002862692"
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; 75820 MW; 4BCB26FCB969272A CRC64;
MKLAVCFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP
ADAIKLNQML SLQPCSNTPP QWRLFRDGEY TLQLDTRSGT PTLMISIQNA VEPVASLVRE
CPKWDGLPLT LDVSATFPEG VAVRDYYSQQ IAIVKNGQIT LQPAASSNGL LLLERAETDA
SAPFDWHNAT VHFVLTDRFE 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 TAKHVELPTW QQLKTEASAA
LREWKKANPD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ
MDTTWQQMAE KLQDFNVLSY LSSHDTRLFR EGGHKAAELL LLAPGAVQIF YGDESSRPFG
PTGSDPLQGT RSDMNWQDVS GKSAASVAHW QKISQFRARH PAIGAGKQTT LSLKQGYGFV
REHGDDKVLV IWAGQQ
//