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Database: UniProt
Entry: B8MDI9_TALSN
LinkDB: B8MDI9_TALSN
Original site: B8MDI9_TALSN 
ID   B8MDI9_TALSN            Unreviewed;       834 AA.
AC   B8MDI9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
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=TSTA_117370 {ECO:0000313|EMBL:EED17952.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED17952.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR   EMBL; EQ962655; EED17952.1; -; Genomic_DNA.
DR   RefSeq; XP_002481944.1; XM_002481899.1.
DR   AlphaFoldDB; B8MDI9; -.
DR   STRING; 441959.B8MDI9; -.
DR   GeneID; 8105795; -.
DR   VEuPathDB; FungiDB:TSTA_117370; -.
DR   eggNOG; ENOG502SMPY; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   InParanoid; B8MDI9; -.
DR   OMA; CESTGVI; -.
DR   OrthoDB; 5486783at2759; -.
DR   PhylomeDB; B8MDI9; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001745; 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   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:UP000001745}.
FT   DOMAIN          391..552
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   834 AA;  91386 MW;  911C945B65995BEC CRC64;
     MTFDVDAVLA KLNQHDKIAL LSGTDFWHTH PIPEHNVPSI RVTDGPNGIR GTKFFAGVPA
     ACLPCGTALG ATWDKSLLRQ AGNLLAQECL AKGAHCWLGP TVNMQRSPLG GRGFESFAED
     PHLSGKLAAA MILGCEQDGS GVISTVKHFV GNDQEHERRA VDCLITPRAL REVYLRPFQI
     VARDANPGAM MTSYNKINGK HVADNRELLE GIVRKEWQWQ PMIMSDWYGT YTTIDAMTAG
     LDLEMPGLSR YRAKYIDSAV QARLIKQSTI DGRARNVLNF VKRGSQARVS PTEKGRDYPE
     DRKLNRTLCS NSIVLLKNEG SILPLPKTIK KIALIGSHVK HPQICGGGSA SLLPYYSVSL
     YDAITEVLPK DAKITYEVGA YTHNMLPVID HMLSGAVMHF YNEPPSIQNR KLLGTEPVTS
     TAFQLMDYNE IPELNRALFW TSLVGDFTPD ISGTWDFGLS VFGTANLYID DELVIDNTSK
     QTRGTAFFGK GTVQVTGSKQ LAKDQKYKLR IEFGSANTTT METIGMVNFG GGAAHLGACL
     RMDAKQMIEN AVRAAANSDC TIICTGLSGE WESEGFDRPH MDLPPGVDEM ITKVLDATQG
     KAVIVNQSGT PVTMAWADKA SCIVQAWYGG NETGHGIADV LFGDVNPCAK LPLSWPVHVR
     DNPAYLSFAS VGGRVLYSED VYVGYKFYEA TGRGVLFPFG YGLSYTSFEL TSSIIAIEPE
     IFDPERPSIV SFRLKNTGQR AGAQIIQLYI SAPNSPTPRP IKELHGFEKV SLAPGEEKTV
     SITIDKYATS LWDEIESMWK SEGGEYEVLV GTSSVDILGK AVLKVPETRY WLGL
//
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