ID   A0A0H3JFX7_ECO57        Unreviewed;       605 AA.
AC   A0A0H3JFX7; A0A6M0JJD6; A0A6M7MRR6; A0A7U8MKR2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Maltodextrin glucosidase {ECO:0000313|EMBL:BAB33876.1};
GN   Name=malZ {ECO:0000313|EMBL:BAB33876.1};
GN   ORFNames=ECs_0453 {ECO:0000313|EMBL:BAB33876.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33876.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33876.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; BA000007; BAB33876.1; -; Genomic_DNA.
DR   RefSeq; NP_308480.2; NC_002695.1.
DR   RefSeq; WP_001302367.1; NZ_VOAI01000005.1.
DR   AlphaFoldDB; A0A0H3JFX7; -.
DR   STRING; 155864.Z0501; -.
DR   GeneID; 914555; -.
DR   KEGG; ecs:ECs_0453; -.
DR   PATRIC; fig|386585.9.peg.553; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_6_4_6; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11338; AmyAc_CMD; 1.
DR   CDD; cd02857; E_set_CDase_PDE_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR017069; MalZ.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF210; MALTODEXTRIN GLUCOSIDASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02903; Alpha-amylase_N; 1.
DR   PIRSF; PIRSF036918; Maltodextrin_glucosidase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
FT   DOMAIN          128..522
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036918-50"
FT   ACT_SITE        374
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036918-50"
FT   SITE            449
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036918-51"
SQ   SEQUENCE   605 AA;  69284 MW;  1B6B30AF60A6393F CRC64;
     MMLNAWHLPV PPFVKQSKDQ LLITLWLTGE DPPQRIMLRT EHDNEEMSVP MHKQRSQPQP
     GVTAWRAAID LSSGQPRRRY SFKLLWHDRQ RWFTPQGFSR MPPARLEQFA VDVPDIGPQW
     AADQIFYQIF PDRFARSLPR EAEQDHVYYH HAAGQEIILR DWDEPVTAQA GGSTFYGGDL
     DGISEKLPYL KKLGVTALYL NPVFKAPSVH KYDTEDYRHV DPQFGGDGAL LRLRHNTQQL
     GMRLVLDGVF NHSGDSHAWF DRHNRGTGGA CHNPESPWRD WYSFSDDGTA LDWLGYASLP
     KLDYQSESLV NEIYRGEDSI VRHWLKAPWN MDGWRLDVVH MLGEAGGARN NLQHVAGITE
     AAKETQPEAY IVGEHFGDAR QWLQADVEDA AMNYRGFTFP LWGFLANTDI SYDPQQIDAQ
     TCMAWMDNYR AGLSHQQQLR MFNQLDSHDT ARFKTLLGRE VARLPLAVVW LFTWPGVPCI
     YYGDEVGLDG KNDPFCRKPF PWQVEKQDMA LFALYQRMIA LRKKSQALRR GGCQVLYAED
     NVVVFVRVLN QQRVLVAINR GEACEVVLPA SPFLNVVQWQ RKEGHGQLTD GILALPAISA
     TVWMN
//