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Database: UniProt
Entry: A0A109MXY8_9BACI
LinkDB: A0A109MXY8_9BACI
Original site: A0A109MXY8_9BACI 
ID   A0A109MXY8_9BACI        Unreviewed;       740 AA.
AC   A0A109MXY8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Glycosyl hydrolase family 65 {ECO:0000313|EMBL:KWW18195.1};
GN   ORFNames=AS888_20310 {ECO:0000313|EMBL:KWW18195.1};
OS   Peribacillus simplex.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1478 {ECO:0000313|EMBL:KWW18195.1, ECO:0000313|Proteomes:UP000064189};
RN   [1] {ECO:0000313|EMBL:KWW18195.1, ECO:0000313|Proteomes:UP000064189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VanAntwerpen02 {ECO:0000313|EMBL:KWW18195.1,
RC   ECO:0000313|Proteomes:UP000064189};
RA   Couger M.B.;
RT   "Genome Sequence of Bacillus simplex strain VanAntwerpen2.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC       {ECO:0000256|ARBA:ARBA00006768}.
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:KWW18195.1}.
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DR   EMBL; LNNH01000023; KWW18195.1; -; Genomic_DNA.
DR   RefSeq; WP_061142476.1; NZ_LNNH01000023.1.
DR   AlphaFoldDB; A0A109MXY8; -.
DR   Proteomes; UP000064189; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KWW18195.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..238
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          299..661
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   DOMAIN          672..730
FT                   /note="Glycoside hydrolase family 65 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03633"
FT   ACT_SITE        473
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT   BINDING         333..334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT   BINDING         573..574
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ   SEQUENCE   740 AA;  83996 MW;  04D818256AC44B1D CRC64;
     MKKLEENSFD PRYINKFASL MTVGNGYFGL RASHEENYVN QTRGMYVAGI YNKATVNEPS
     DLVNLPDVAG MNIELDGEVF SLLTGEILSY KRQLNLENGE LRRDILWKSR TGSRFRLTFQ
     RFAAKNDRHV LATKLTVTSL DKPAQMKIVT GIDAQQTNFG RQHLIEEKVR VAEGDLLQGT
     YKTTESGHTI AIATCCTGSV KGEMSHTAKN RQLLSAINQN LLADTPFVLE KMSVIFTSLD
     GDLRGESPEE ATEAVLRSCS AVGYDALLHK SAGEWAQFWM EKRIKVASTR DFDQLAIDFS
     LYQLEVMTPA HDERFSVGAK GLTGEGYKGH VFWDTEIFIT PFHLYTEPEK ARKLLRYRYL
     RLKQALDKAA TNGYEGALFP WESAFTGEEE TPEFAAINIK TGKRQKVASA LAEHHIVADI
     AYTVVKYYQN TWDDWFMKKE GLELLKETSR FWISRAVEEN DQLVIKDVIG PDEYTEHIDN
     NAFTNYMAWY NVEQALFFMD KYGDDDRQLK DRGHEFLKRL YLPKANDDKI IPQDDTFLSK
     PEIDLSRYKQ AQGSQGILMD YSRQEVNEMQ ILKQADVVML LYLLPDVFPS DIIYENLRYY
     EEHTIHDSSL SKAIHAIVAA RAGEIEKAYE FFQESCLIDL GPNPQSSDEG LHAASLGAIW
     MAAMFGFANV SIKNQRLSLD PKLPSGWSEL AFPLIFQGSR LHIALTHNQA VITKVSGDDV
     CIELNGTEFL VSDKFAMDLH
//
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