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Database: UniProt/TrEMBL
Entry: B2U552_SHIB3
LinkDB: B2U552_SHIB3
Original site: B2U552_SHIB3 
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
//
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