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Database: UniProt
Entry: A0A268E7B1_9BACI
LinkDB: A0A268E7B1_9BACI
Original site: A0A268E7B1_9BACI 
ID   A0A268E7B1_9BACI        Unreviewed;       559 AA.
AC   A0A268E7B1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=oligo-1,6-glucosidase {ECO:0000256|ARBA:ARBA00038939};
DE            EC=3.2.1.10 {ECO:0000256|ARBA:ARBA00038939};
GN   ORFNames=CHH83_10920 {ECO:0000313|EMBL:PAD69020.1};
OS   Bacillus sp. 7586-K.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD69020.1, ECO:0000313|Proteomes:UP000216230};
RN   [1] {ECO:0000313|EMBL:PAD69020.1, ECO:0000313|Proteomes:UP000216230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7586-K {ECO:0000313|EMBL:PAD69020.1,
RC   ECO:0000313|Proteomes:UP000216230};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some
CC         oligosaccharides produced from starch and glycogen by alpha-amylase,
CC         and in isomaltose.; EC=3.2.1.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00036217};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAD69020.1}.
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DR   EMBL; NPCL01000033; PAD69020.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268E7B1; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000216230; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 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; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF184; OLIGO-1,6-GLUCOSIDASE 1; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:PAD69020.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216230}.
FT   DOMAIN          13..419
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   559 AA;  65630 MW;  27A6A9FD84C9205C CRC64;
     MNKAWWKESV VYQIYPRSFM DSNGDGIGDL QGIISKLDYI KNLGIDVIWL SPVYKSPNDD
     NGYDISDYQD IMDDFGTMAD WEQLLAEVHK RGMKLIMDLV VNHSSDEHPW FLEARQSKDS
     KYRDYYIWRK GKNGKEPSSW YSNFGGSAWE YDEATDEYYL HLFSKKQPDL NWRNPSLRKE
     IFNMMKWWLE KGIDGFRMDV INFISKPENF EDGDLKPGKK YASGSKFYRN GPHIHDYLQE
     MNREVLSHYD VMTVGEMPGV TPELAKLYTS EDRKELNMVF QFEHMGLDNG ENGKWDLKPL
     KLADLKANLS KWQLALEDTG WNSLYFNNHD QPRSVSRFGN DKKYRVESAK MLATLLHMMK
     GTPYVYQGEE IGMTNIRFDS IEDYRDIEII NMFKEQTEAG IPHQQIMESI YAKGRDNSRT
     PMQWDASPNA GFTTSTPWLK VNPNYIEINA EAEISNANSI YHYYRKLIQL RKKYDVIVYG
     KYELLLPEHQ EIFAYTRTLG DEKLLVICNF YEGQPMFELP EHITYQSAEL LISNYPEKLT
     HELESIQLRP YDASVFLLK
//
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