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Database: UniProt
Entry: A0A2N5MGJ1_9BACI
LinkDB: A0A2N5MGJ1_9BACI
Original site: A0A2N5MGJ1_9BACI 
ID   A0A2N5MGJ1_9BACI        Unreviewed;       563 AA.
AC   A0A2N5MGJ1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=oligo-1,6-glucosidase {ECO:0000256|ARBA:ARBA00038939};
DE            EC=3.2.1.10 {ECO:0000256|ARBA:ARBA00038939};
GN   ORFNames=CUU64_14075 {ECO:0000313|EMBL:PLT33415.1};
OS   Bacillus sp. V5-8f.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2053044 {ECO:0000313|EMBL:PLT33415.1, ECO:0000313|Proteomes:UP000235260};
RN   [1] {ECO:0000313|EMBL:PLT33415.1, ECO:0000313|Proteomes:UP000235260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V5-8f {ECO:0000313|EMBL:PLT33415.1,
RC   ECO:0000313|Proteomes:UP000235260};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant Strains Isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-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:PLT33415.1}.
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DR   EMBL; PGUW01000011; PLT33415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5MGJ1; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000235260; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; 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:PLT33415.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235260}.
FT   DOMAIN          15..422
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   563 AA;  66337 MW;  31040DC4396A29DC CRC64;
     MSQNKKWWKE SVVYQIYPRS FMDSNGDGIG DIPGIISKLD YLKHLGVDVV WLSPVYQSPN
     DDNGYDISDY QEIMEEFGTM EDWDRLLDEM HKREIKLVMD LVVNHTSDKH AWFMEARNSK
     DNPYRDYYIW RQGRGGLPPT DWEGSFGGSA WEYSPETEEY YLHMFSKKQP DLNWENPALR
     NDIYSMMKFW LDKGIDGFRM DVINMISKKE FLPTYEELAE GTAKPLPYQF NGASVHDYLQ
     EMNREVLSKY DIMTVGECPK VTPEQAELYT AEERNELNMV FQFEHMSLDK QKGKQKWDLK
     TLELSDLKQN LSKWQKQLEN RGWNSLYWNN HDQPRIVSRF GTDGKYRVES AKMLATLLHF
     MKGTPYIYQG EEIGMTNVRF PGIEDYQDIE TKNMYQERVH ELGYDSKDVM ESIYAKGRDN
     ARTPMQWDDS EHAGFTKGTP WFNVNPNYTA INVKNDLENK NSIFYHYKKL IELRKKHEIV
     VYGSYDLILG DHESIFAYIR QLGDQMLLVI NNFYEKEAEF ELPSSITFGS GELLISNYDD
     HNVADIAKFT LRPYESVVYQ LEK
//
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