ID A0A1F8A5Y6_9EURO Unreviewed; 1366 AA.
AC A0A1F8A5Y6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=ABOM_003945 {ECO:0000313|EMBL:OGM47146.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM47146.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM47146.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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 -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992}.
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:OGM47146.1}.
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DR EMBL; LYCR01000025; OGM47146.1; -; Genomic_DNA.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
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 Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
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 Pfam; PF00083; Sugar_tr; 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 SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS51820; PA14; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 931..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 984..1006
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1027..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1053..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1139..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1181..1198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1205..1223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1235..1254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1305..1324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 390..549
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT DOMAIN 878..1328
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 1366 AA; 151478 MW; 08A34EFAEB40270C CRC64;
MTLDIDYVFS PALSIKSRVS AKTKPGTDFW HTHPIPEFNV PSIRSTDGPN GIRGTKFFAG
VPAACLPCGT ALASAWDQDL LRDAGILIGK ECLAKGAHCW LGPTINMPRS PLGGRGFESF
AEDPHLAGGM AAAMITGCES TGVISAVKHF VGNDQEHERR AVDVLVTQRA LREIYLRPFQ
IVARDACPGA LMTSYNKING KHVVESKEML DMVRQEWKWN PLIMSDWLGT YTTIDSMNAG
LDLEMPGPSR YRGRYVESAL QARLIKESTI DSRARRVLEF VQQASRASVS AVETGRDYPE
DRALNRKLCA DSIVLLKNKN DLLPLPKTIK KIALIGSHVR TPAISGGGSA SLEPYYAVSL
YDAVSEALPH TEILHEVGAY AHKMLPVIDR LLENAVMHFY NEPIGTERIL RATQPMSKTA
FQLMDFSAPE LNRGLFYTTL TGDFTPDVSG VWDFGLTVFG TGTLYVDDEL VVDNTTHQTR
GTAFFGKGTV QELGSKTLNA GQTYKIRIEY GSANTSPMKA IGVVHFGGGA AHLGACLHVD
PAEMVRSAVK AAAEAEYTVL CTGLNHEWES EGFDRPDMDL PPGIDALIAS VLEVAAHKTV
IVNQSGTPVT MPWADRARGI VQAWYGGNET GHGIADVIFG DVNPSGKLPL SWPLDVKHNP
AYLNYASVGG RMLYGEDVYV GYRYYEKVGR EVLFPFGHGL SYTTFTVRPD VVFSQEAFRP
EQPPTAAVQI KNTGKVAGAQ VLQLYISAPQ SPTPRPVKEL HGFAKVYLHP GEERVVHIRM
DKYATSFWDE IEGMWKSEEG VSVSEVTGHG TVRLIYKDDQ RLDYSRHPRV SISEAVNMVV
VGKQRDEDVS EPVLANLLAE DRTAWYKKPN LRRLYLILFP ACMGIEITSG FDSQIINTVQ
IVYTWNKYFG RLTGDTVDGK PEYQVEPNLK GFLGAAYSLG AILALPLVPW VNQRLGRRWT
IMFGSCISLV GAILQGFANG VGMYVVARML LGFGIPFCIV AGSSLIGELG YPKERPILTS
LFNSSYFIGQ IVAAAVGLGT VTIASNWAWR IPSLLQIAPA MVQVVFVFFL PESPRYLISK
DRHEEAFDIL VKYHAEGDRS SVIVRAEIAQ IERTIKLELE AAKQTWWDMF RTAGMRRRMF
ISAFLGLFTQ WSGNTLISYY LSDLLALVGI TDSVIKSKIN IGIACWGLVS GTTLALTAPR
FKRRTMYLTC AISLLCVYIG WTISMERFMT TKVKAAAILT IFFIFAYSPA YNLGYNALTY
TYLIEIFPYL GRSRGLSWFQ FYGRGATFFA TYVNPVGLDR IKWRWLLVYC CWLAFEVVFI
YFFFPETSGR TLEELSFMFE GKEKANEVAA AVHKQIEGDE KKADQA
//
