ID A0A512UKW4_9ASCO Unreviewed; 836 AA.
AC A0A512UKW4;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=JCM33374_g5375 {ECO:0000313|EMBL:GEQ71689.1};
OS Metschnikowia sp. JCM 33374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=2562755 {ECO:0000313|EMBL:GEQ71689.1, ECO:0000313|Proteomes:UP000319698};
RN [1] {ECO:0000313|EMBL:GEQ71689.1, ECO:0000313|Proteomes:UP000319698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 33374 {ECO:0000313|EMBL:GEQ71689.1,
RC ECO:0000313|Proteomes:UP000319698};
RA Hirao A.S., Imai R., Endoh R., Ohkuma M., Degawa Y.;
RT "Draft genome sequence of a novel Metschnikowia sp. strain JCM 33374, a
RT nectar yeast isolated from a bumblebee.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448,
CC ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:GEQ71689.1}.
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DR EMBL; BIMT01000129; GEQ71689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A512UKW4; -.
DR STRING; 2562755.A0A512UKW4; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000319698; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361161};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000319698}.
FT DOMAIN 399..558
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 836 AA; 91973 MW; 2693CF98B08C30F0 CRC64;
MAVIDVENVL SELTLTEKIG LISGIDFWHT YAVKRLGVPS VRVSDGPNGV RGTKFCNGIP
AACFPCGTGM ASTFNKELLY EAGALMAKEA KAKSASCILG PTTNIQRGPL GGRGFESFSE
DPYLAGMASA SVINGMQDND IASALKHFVC NDLENERSAS DSVVTERALR EIYLEPFRLA
VKYSNPVSFM TSYNKVNGEH VSQSKKFLKD ILRNEWGWEG LIMSDWLGVY TSKAAIENGL
DLEMPGPSIF RNQGTISHMV SSKELCISDL DDRVRNVLNF VNWCSRSNAV EYGPETQNNN
PETREVLNKI ATEGIVLLKN EDHLLPLNKD ENIAVIGPNA KFAAYCGGGS AALPTYYCTN
PYDSISAKLG RKPEYSLGCY GHKSLPGIAE SPLSRNPVTG EPGINVRFFE KPCSGEARSQ
FDEFQYSRSP LVLFDYSHPQ IVDNLYYCEI TTEITPQESG NYDFSLTVCG TAQLFVDGML
VVDNTVNQKS GTAFFGAGTA EVIESIFLNA GQTYSVVVQF GSGKTSSLNR ESALAFGSAI
CIGFCKVIDV ETEIQKAISL ASRVDKVVLT IGLNLEWESE GFDRPDMNLP PFTDELVRAV
LKANPNTIIV NQSGTPVEMP WLQDVKALVH ASYGGSESGN AIANVLFGDA NPSGKLPLSW
PLRNVDNPAF LNFKTVRGRV LYGEDIYVGY RFYEKLERSV AFPFGYGKSY TSFTLLDLDV
MVDEDLDTLV ATLSIENTGD CDGTETVQLY IAPQGQHVQR PVKELKGFEK LFLKPGTKKL
VKFNLSLKDS ASYFDEYLAK WNLEKGDYEV QVGTSSKDID LRYRFTVQKD KLWVGL
//