ID   A0A218VUN3_PUNGR        Unreviewed;       407 AA.
AC   A0A218VUN3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Beta-glucosidase 12-like {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CDL15_Pgr005993 {ECO:0000313|EMBL:OWM63731.1};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM63731.1, ECO:0000313|Proteomes:UP000197138};
RN   [1] {ECO:0000313|Proteomes:UP000197138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX   PubMed=28654223; DOI=10.1111/tpj.13625;
RA   Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA   Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT   "The pomegranate (Punica granatum L.) genome and the genomics of
RT   punicalagin biosynthesis.";
RL   Plant J. 91:1108-1128(2017).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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:OWM63731.1}.
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DR   EMBL; MTKT01005880; OWM63731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218VUN3; -.
DR   Proteomes; UP000197138; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF344; THIOGLUCOSIDASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE   3: Inferred from homology;
FT   ACT_SITE        306
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   407 AA;  46702 MW;  DAB883829D5B108E CRC64;
     MADKWASNKA SDGKVSKGVN QQGINFYNSL IDELLAYGIQ PFVTLFHWDV PQTLEDKYGG
     FLSREIVDDF HDYADLCFKE FGDRVKYWTT LNEPNNFAQF GYATGTYAPG RCSNYIGNCT
     NGNSATEPYI VAHHLLLSHA SVVQLYRSKY QTSQKGKIGL GTSTYWMKPK FPTDQSRDAA
     MRALDFQFGW IVDPITFGDY PKSMRNLVGT RLPNFTIAES KMLRGSYDYL GVNYYTARYV
     DESTSYSTTN LSYTTDGRCN LTTERDGITI GKPTPVVWIY MYPKGIRDLM HYVKNKYNPS
     VIYILENGVG DANNVTLSLK DALRDTLRMK YHKLHLFYLS KAIEEGVNVK GYLTWSFLDN
     FSWALGYTVR YGVIFIDYKN GLKRYPKDSS LWFKQFLRAE NTTHPHI
//