ID B2U552_SHIB3 Unreviewed; 676 AA.
AC B2U552;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Alpha-amylase, periplasmic {ECO:0000313|EMBL:ACD10383.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:ACD10383.1};
GN Name=malS {ECO:0000313|EMBL:ACD10383.1};
GN OrderedLocusNames=SbBS512_E3951 {ECO:0000313|EMBL:ACD10383.1};
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609 {ECO:0000313|EMBL:ACD10383.1, ECO:0000313|Proteomes:UP000001030};
RN [1] {ECO:0000313|Proteomes:UP000001030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512 {ECO:0000313|Proteomes:UP000001030};
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001063; ACD10383.1; -; Genomic_DNA.
DR RefSeq; WP_000761942.1; NC_010658.1.
DR AlphaFoldDB; B2U552; -.
DR STRING; 344609.SbBS512_E3951; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; sbc:SbBS512_E3951; -.
DR HOGENOM; CLU_022115_1_0_6; -.
DR OMA; DKVMVVW; -.
DR Proteomes; UP000001030; 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:ACD10383.1};
KW Hydrolase {ECO:0000313|EMBL:ACD10383.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001030};
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_5002781207"
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; 75838 MW; 63A89F1F5BA63776 CRC64;
MKLASCFLTL LPGFAVAASW TSPGFPVFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP
ADAIKLNQML SLQPCSNTPP QWRLFRDGKY TLQIDTRSGT PTLMISIQNA AEAVANLVRE
CPKWDGLPLT LDVSATFPEG AAVRDYYSQQ IAIVKNGQIT LQPAATSNGL LLLERAETDT
SAPFDWHNAT VYFVLTDRFE NGDPSNDQSY GRHKDGMAEI GTFHGGDLRA LINKLDYLQQ
LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGNE ADLRTLVDSA
HQRGIRILFD VVMNHTGYAT LADMQEYQFG ALYLSGDEVK KTLGERWSDW KPAAGQTWHS
FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STTASGLPVF
YKNKTDTHAK VIEGFTPRDY LTHWLSQWVR DYGIDGFRVD TAKHVELPAW QQLKTEASSA
LREWKKTNPD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ
MDTTWQQMAE KLQGFNVLSY LSSHDTRLFR EGGDKAAELL LLAPGAVQIF YGDESSRPFG
PTGSDPLQGT RSDMNWQDVS GKSAANVAHW QKISQFRARH PAIGAGKQTT LSLKQGYGFV
REHGDDKVLV IWAGQQ
//