ID C4Y1N8_CLAL4 Unreviewed; 837 AA.
AC C4Y1N8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=CLUG_02120 {ECO:0000313|EMBL:EEQ37997.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ37997.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ37997.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ37997.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
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DR EMBL; CH408077; EEQ37997.1; -; Genomic_DNA.
DR RefSeq; XP_002618661.1; XM_002618615.1.
DR AlphaFoldDB; C4Y1N8; -.
DR STRING; 306902.C4Y1N8; -.
DR GeneID; 8499320; -.
DR KEGG; clu:CLUG_02120; -.
DR VEuPathDB; FungiDB:CLUG_02120; -.
DR HOGENOM; CLU_004542_4_0_1; -.
DR InParanoid; C4Y1N8; -.
DR OMA; TYYVDME; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000007703; 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:UP000007703}.
FT DOMAIN 400..559
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 837 AA; 92489 MW; 070FE3D9C181DC31 CRC64;
MADIDVEKVL SELTLAEKIG LTAGVDFWHT YKVERLGVPT LRLSDGPNGV RGTKFVNGAP
SACFPCGTGL ASTFNKDLLY KAGRLMADEA KHKSAHVILG PTTNMQRGPL GGRGFESFSE
DPHLAGMASA SIVKGMQDND IAATIKHFVC NDLEHERNSS DAIVTERALR EIYLEPFRLA
VKYADPKSFM TAYNKVNGEH VSQSHRILEQ ILREEWNWDG LVMSDWYGAY TAKESLTNGL
DLEMPGPSGM RTVQNISHMV NSRELNIKYL DERVRNVLKL VKWCARSKLE ERGPETTENN
TPETRALLNK IASESVVLLK NNDSVLPLKK EESIAVIGPN AKFAAYCGGG SASLLSYYTT
TPYDAIKEKL GHEPKYAVGC YAHQMLPGFS LSPYTKNPVT GKSGVNCKLY NDAPGTKNRR
QFDEFDITMS PIILFDYRHP AIVDELFYMD ITGDLTPEES GEYEFSLTVS GTAQLFIDDK
LVIDNKNSQT LGTAFFGTGT IEMKQKVPLD AGKTYNVRVE FGSSKTSKLR PSSVISFGGC
VSIGMCKVID PKEEIAKAVE LAKSVDKVVL SIGLNAEWES EGFDRPDMEL PLLTNDLVEA
VLAANPNTVV VNQSGTPVEM PWLSKANALV HAWYGGSEAG NAIANVLFGD VNPSGKLSLS
WPFKNSDNPA YLNFHTERGR VLYGEDIYIG YRFYDKLQRR VAFPFGYGLS YTTYKYSDLN
VTVNEEDDSL TASVTVENTG SKDGAETVQF YVAPKTSEVA RPVKELKGFD KVFVKAGEKA
TAKVQLSLKD SASFFDEYHD KWSLEKGTYE VQVGKSSDDV ELIQEFKVKE SKLWSGL
//
