BTGE_ASPFU
ID BTGE_ASPFU Reviewed; 565 AA.
AC Q4WC60;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Probable beta-glucosidase btgE;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase btgE;
DE AltName: Full=Cellobiase btgE;
DE AltName: Full=Gentiobiase btgE;
DE Flags: Precursor;
GN Name=btgE; ORFNames=AFUA_8G05610;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose (By similarity).
CC {ECO:0000250}.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC Note=Covalently-linked to the cell wall. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL85324.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000013; EAL85324.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_747362.1; XM_742269.1.
DR AlphaFoldDB; Q4WC60; -.
DR SMR; Q4WC60; -.
DR STRING; 746128.CADAFUBP00007978; -.
DR GeneID; 3504706; -.
DR KEGG; afm:AFUA_8G05610; -.
DR eggNOG; ENOG502QS0R; Eukaryota.
DR HOGENOM; CLU_027285_2_1_1; -.
DR InParanoid; Q4WC60; -.
DR OrthoDB; 1142019at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000002530; Chromosome 8.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall; Cellulose degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..565
FT /note="Probable beta-glucosidase btgE"
FT /id="PRO_0000395133"
FT REGION 246..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 405
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 501
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
SQ SEQUENCE 565 AA; 58148 MW; 4D06B871D8835ACC CRC64;
MRGAILATAA ALAGTAMADV AHMRRHGHDS FHQRRSPLAE ADATCGCTTE VVTVWGPPTL
IPVASPTPST VTSEAVTTLH STSTTTVTVI ASASTPAASP SPATDKVPLP TPAITNFPST
GVYTIPATTV TVFDTTTVCG ATTTELPAGT HTYGGVTTVV ETATTVVCPY ATVEPSGTTV
TSVIKTTTYV CPSAGTYTIA PTTTTVPTST VIVYPTPAVI TPGTYTQPEQ TVTVTRTDYT
YVCPFTGQDE PTSAPAAPST TAVPATTTAA PETTTAAPDT TTAVPSTSSA APSSSSTAPA
STGAVSGQMG MTYTPYTKGG DCKDKSSVLS EVAALKSKGF THVRVYSTDC NSLEYIGEAA
RTSGLQMIIG VFISSTGVSG AQDQVTAISK WAQWDLVSLI VVGNEAIQNG YCDASTLAGF
ISSAKSAFQA AGYTGKVTTT EPINVWQAHG STLCGVCDIV GANIHPFFNA DVSADQAGKF
VAQEIKVLES ICPGKDVLNL ETGWPHAGNA NGKAVPGTSE QAIAIKSIAD EVGSKSVFFS
YFDDLWKEPG QFGVERYWGC FDTFN
