ID C4YF10_CANAW Unreviewed; 479 AA.
AC C4YF10;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN ORFNames=CAWG_01120 {ECO:0000313|EMBL:EEQ42896.1};
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ42896.1, ECO:0000313|Proteomes:UP000001429};
RN [1] {ECO:0000313|EMBL:EEQ42896.1, ECO:0000313|Proteomes:UP000001429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1 {ECO:0000313|EMBL:EEQ42896.1,
RC ECO:0000313|Proteomes:UP000001429};
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=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; CH672346; EEQ42896.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YF10; -.
DR PaxDb; 5476-C4YF10; -.
DR VEuPathDB; FungiDB:CAWG_01120; -.
DR HOGENOM; CLU_004624_0_1_1; -.
DR OMA; GWDMQDL; -.
DR Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..479
FT /note="glucan 1,3-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002944669"
FT DOMAIN 95..348
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 479 AA; 54593 MW; 9F9BE6601DCCB006 CRC64;
MMLFLIHLMA LCCMFVAEVA CEQFNSTSNS SSVQSSLIDF QYKGVSIGGW LVLEPYITPS
LFNATLSSGE TWTDLPVDEY HFCEKLGAKE AEKRLTDHWE SMYNETDFKQ IKEAGLNMVR
IPIGYWSFEK LEGDPYVSGA QDYLDKAIEW SHANDLKVMI DLHGAPNTQN GFDNSGLRNL
GYPGWQNKTE YVNHTYKVLQ QMFQKYGTGK YASDYKNTII GIEVLNEPLN PNMDKLKEFY
IESYNDGREI QVINNTIFFQ EAFQPIGYWD SFLEKGEIKV TETSNGTNHT TTKKADFKNI
IIDHHHYEVF TESQVASNVS THLENIKNYA SAIGKEKAKA IVGEWSAALT DCAPWLNGIG
LGSRYEGTAP YTNDRVGSCA EFNKSPDKWS KKQKKDYRRF VEMQLYEYST NSQGWIFWCW
KTEGATEWDF RALVKNGIMP QPLDNYKYVK NGTDTSSASA IASNKMTLLL AYLLVILVI
//
