(data stored in SCRATCH zone)

SWISSPROT: C8U287_ECO10

ID   C8U287_ECO10            Unreviewed;       605 AA.
AC   C8U287;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   SubName: Full=Maltodextrin glucosidase {ECO:0000313|EMBL:BAI29245.1};
GN   Name=malZ {ECO:0000313|EMBL:BAI29245.1};
GN   OrderedLocusNames=ECO103_0377 {ECO:0000313|EMBL:BAI29245.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29245.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29245.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|SAAS:SAAS00964676}.
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DR   EMBL; AP010958; BAI29245.1; -; Genomic_DNA.
DR   CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; BAI29245; BAI29245; ECO103_0377.
DR   KEGG; eoh:ECO103_0377; -.
DR   HOGENOM; HOG000055363; -.
DR   KO; K01187; -.
DR   OMA; TPDWVKH; -.
DR   Proteomes; UP000000959; 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; cd02857; E_set_CDase_PDE_N; 1.
DR   Gene3D; 2.60.40.1180; -; 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   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; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U287.
DR   SWISS-2DPAGE; C8U287.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959}.
FT   DOMAIN      128    522       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    337    337       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR036918-50}.
FT   ACT_SITE    374    374       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR036918-50}.
FT   SITE        449    449       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR036918-51}.
SQ   SEQUENCE   605 AA;  69237 MW;  0F80F1E4C1ED865D CRC64;
     MMLNAWHLPV PPFVKQSKDQ LLITLWLTGE DPPQRIMLRT EHDNEEMSVS MHKQRSQQQP
     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 VRHWLKAPWS MDGWRLDVVH MLGEAGGARN NMQHVAGITE
     AAKETQPEAY IVGEHFGDAR QWLQADVEDA AMNYRGFTFP LWGFLANTDI SYDPQQIDAQ
     TCMAWMDNYR AGLSHQQQLR MFNQLDSHDT ARFKTLLGRD IARLPLAVVW LFTWPGVPCI
     YYGDEVGLDG KNDPFCRKPF PWQVEKQDTA LFALYQRMIA LRKKSQALRR GGCQVLYAED
     NVVVFVRVLN QQRVLVAINR GEACEVVLPA SPFLNVAQWQ RKEGHGQLTN GILALPAISA
     TVWMN
//

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