ID BGLH_ASPFU Reviewed; 829 AA.
AC Q4WL79;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Probable beta-glucosidase H;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase H;
DE AltName: Full=Cellobiase H;
DE AltName: Full=Gentiobiase H;
GN Name=bglH; ORFNames=AFUA_6G14490;
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
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 / CBS 101355 / FGSC A1100 / Af293;
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL89285.1; -; Genomic_DNA.
DR RefSeq; XP_751323.1; XM_746230.1.
DR AlphaFoldDB; Q4WL79; -.
DR SMR; Q4WL79; -.
DR STRING; 330879.Q4WL79; -.
DR GlyCosmos; Q4WL79; 6 sites, No reported glycans.
DR EnsemblFungi; EAL89285; EAL89285; AFUA_6G14490.
DR GeneID; 3508640; -.
DR KEGG; afm:AFUA_6G14490; -.
DR VEuPathDB; FungiDB:Afu6g14490; -.
DR eggNOG; ENOG502SMPY; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR InParanoid; Q4WL79; -.
DR OMA; DVKHNPA; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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; 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:SF17; BETA-GLUCOSIDASE H-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; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted.
FT CHAIN 1..829
FT /note="Probable beta-glucosidase H"
FT /id="PRO_0000394879"
FT DOMAIN 389..548
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT ACT_SITE 225
FT /evidence="ECO:0000250"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 829 AA; 90990 MW; 9FC9D770D59A9ED9 CRC64;
MTPKFDIDYV LANITEDDKI ALLSGSDFWH THAIPKFNVP PIRTTDGPNG IRGTKFFAGV
PAACLPCGTA LGATWDRDLL HQAGVLLGKE CLAKGAHCWL GPTINMQRSP LGGRGFESFA
EDPHLSGIMA KSIILGCEST GVISTVKHYV GNDQEHERRA VDVLVTPRAL REIYLRPFQI
VARDAHPGAL MTSYNKINGK HVVENPAMLD IVRKDWHWDP LIMSDWLGTY TTIDSLNAGL
DLEMPGPTRY RGKYIESAMQ ARLIKQSTIS KRARKVLEFV ERASRAPVSA DETGRDFPED
RALNRTLCAN SIVLLKNDGN LLPIPKTVKK IALIGSHVKT PAISGGGSAS LEPYYAVSLY
DAVVEALPDA EILYEAGAYA HRMLPVIDRM LSNAVIHFYN EPPEKERTLL ATEPVVNTAF
QLMDYNAPGL NRALFWATLI GEFTPDVSGL WDFGLTVFGT ATLFIDDEMV IDNATRQTRG
TAFFGKGTVQ EVGQKQLTAG QTYKIRIEFG SANTSPMKAI GVVHFGGGAA HLGACLHMDP
EQMVANAVRV AAEADYTIVC TGLNRDWESE GFDRPDMDLP PGIDALISSV LDVAADRTVI
VNQSGTPVTM PWAHRARGIV QAWYGGNETG HGIADVLFGD VNPSGKLPLS WPADVRHNPT
YLNNMSVGGR MLYGEDVYIG YRFYEKVGRE VLFPFGHGLS YTTFHVSPEA TVSPIVFSSD
SPPTATVLVK NTGPMAGAQT LQLYIAAPNS ATPRPVKELH GFTKVFLQSG EERSVSIHID
RYATSFWDEI EDMWKSEEGV YQVLIGTSSQ EIVSRGEFRV EQTRYWRGV
//
