ID A0A401KYP2_ASPAW Unreviewed; 856 AA.
AC A0A401KYP2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Probable beta-glucosidase M {ECO:0000256|ARBA:ARBA00039571};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase M {ECO:0000256|ARBA:ARBA00041282};
DE AltName: Full=Cellobiase M {ECO:0000256|ARBA:ARBA00041589};
DE AltName: Full=Gentiobiase M {ECO:0000256|ARBA:ARBA00041805};
GN ORFNames=AAWM_07227 {ECO:0000313|EMBL:GCB24342.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB24342.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB24342.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB24342.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) 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 -!- 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:GCB24342.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDHI01000017; GCB24342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KYP2; -.
DR STRING; 105351.A0A401KYP2; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF5; BETA-GLUCOSIDASE M-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000286921};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..856
FT /note="Probable beta-glucosidase M"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019526510"
FT DOMAIN 748..814
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 856 AA; 93485 MW; 15820D4C6784BC90 CRC64;
MVRLFVHALL LLVGSSLAIA QRPEIPDDIP LDKGTRDYLE SLPPDELAAV LEVYQEAFAG
QVPAPPELIT QQELSLYGKS PAVYPSPLAK GTGTWADAYA HVKALVNQMT NEEKANTTSL
SDSGVPAIPR LGFPGLRLHD GPNGLNALEE VTAYASGITV GASWNKDLAH ARGQSMGKGA
RRKGATCWDR LLVRLAGQRP GGRNWESFSV DPYLCGQMGA KTVLGIQENV IATAKHFVLN
EQETDRNPSM FGFSNASVSS NIDDKTMHEY YLWPFQDAVK AGVGSVMCSY QRVNGSHSCQ
NSWTQNGLLK TELGFQGYII SDYNARWGGI ASTQAGMDLV TPPSAVWPQN LTIAVENGTL
AESRLDDMVI RILTSWFKFA QFDPANPLGL PPNISKAHEG SSSIDPSPEA KYIIRQGAVE
GAVLVKNVNN TLPLKKPKIL SLFGYDAHAP LVNSPTGVNS KYSIGYQSVN RTKVQVQGLF
VGVGECPSAA TLGTLVGGGG SGSVTPQYIN SPFDAFQQRA YEDGTFLYWD FDSEDPSYSE
SDACLVFINE FASEIVDRVS LADQYSDNLV MNVAKKCRNT IVSIHNAGVR LVDRWIDHPN
VTAVIFAHLP GQDAGPALVD IMYGEQAPSG KLPYTVAKNE SDYSEELLWP VRPDNSSNYY
THADFTEGSY IDYRRFDALN IEPRFEFGFG LTYTTFNYSD LEVRHTEANS SFYPPPGEVM
EGGLESLWDV VAIVTARVSN TGEVTASEIP QLYVGIPGAP IKQLRGFEKI PLHPKEGKSV
SFPLTRRDLS LWDTESQSWY LERGEYKLYV DLLALADGDQ ILGIVAGSNV YQDENCTPIT
VPNAPSLSDL FCDKIS
//
