ID A0A072PL80_9EURO Unreviewed; 841 AA.
AC A0A072PL80;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Probable beta-glucosidase H {ECO:0000256|ARBA:ARBA00039581};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase H {ECO:0000256|ARBA:ARBA00041278};
DE AltName: Full=Cellobiase H {ECO:0000256|ARBA:ARBA00041602};
DE AltName: Full=Gentiobiase H {ECO:0000256|ARBA:ARBA00041806};
GN ORFNames=A1O9_04958 {ECO:0000313|EMBL:KEF60108.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF60108.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF60108.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF60108.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00024983}.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KEF60108.1}.
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DR EMBL; AMGV01000003; KEF60108.1; -; Genomic_DNA.
DR RefSeq; XP_013262698.1; XM_013407244.1.
DR AlphaFoldDB; A0A072PL80; -.
DR STRING; 1182545.A0A072PL80; -.
DR GeneID; 25279885; -.
DR VEuPathDB; FungiDB:A1O9_04958; -.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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 {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT DOMAIN 388..549
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 841 AA; 91691 MW; CC752367E5A6EB4C CRC64;
MAFDVDTVFP QLKQADKIAL LSGIDFWHTH PIPAHNVPSV RFTDGPNGIR GTKFFAGVPA
ACLPCGTALG ATWDKALLRQ AGKLLGDECI AKGAHGWLGP TVNMQRSPLG GRGFESFSED
PHLAGTIAAS MILGCESTGV ISTVKHFIGN DQEHERRAVD CLIAPRAFRE VYLRPFQIVA
RDANPGALMT SYNKINGRHV VDNAEMLQGI VRDEWKWDPL IVSDWYGTYT TIDAMVAGLD
LEMPGVSRYR GKYIESAVQA RLIKQSTIDA RARRVLKFVH RASQVKVSEE QVGRNYPEDR
ALNRLVSSNS IVLLKNDSSI LPLPKTLKKI ALIGSHVKMP AISGGGSATL LPYYTVSLHD
AVTEAVPEAT ITHEVGAYAH NMLPAIDSLL HNAVINFYNE PPKVTDRKLL GIEHVTSATF
QLMDYNGIPA LNRALFWGSL VGEFIPDATG TWDFGLTVFG TANLYLDDEL IIENTIHQTR
GTAFFGKGTT EKFGSRVLEA GKSYNIRIEF GNANTTTMET IGMVNFGGGA AHLGACLRLG
PDEMIERAVQ AAKDAEQTII CTGLSGEWES EGFDRPHMDL PPGIDEMISQ VIAVAPTAVI
INQSGTPITM PWADQAKCIV QAWYGGNEAG HGMSDVLFGD VNPSGKLPLS WPVSVKHNPA
YLNYASVGGR VLYGEDVYVG YKFYEKTDRE VLFPFGQVTP PSSFLLQHGL SYTTFALTSP
EVQVDPVEFA PENPSVAIIK IKNTGPVAGQ QVVQLYVAAP SSPTPRPVKE LHGFEKIVLQ
PGEEKEVTIA VDKYATSFWD EIESMWKSEA GTYEVLVGTS SQEILGKGTL VVPETRYWLG
L
//
