UniProt: A0A512UKW4

Database: UniProt
Entry: A0A512UKW4_9ASCO

LinkDB:  A0A512UKW4_9ASCO 
Original site:  A0A512UKW4_9ASCO

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
All databases (23)   

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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
//

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