ID A0A089JSP9_9BACL Unreviewed; 929 AA.
AC A0A089JSP9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:AIQ23939.1};
GN ORFNames=H70737_14325 {ECO:0000313|EMBL:AIQ23939.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ23939.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ23939.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ23939.1,
RC ECO:0000313|Proteomes:UP000029519};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; CP009279; AIQ23939.1; -; Genomic_DNA.
DR RefSeq; WP_042188130.1; NZ_CP009279.1.
DR AlphaFoldDB; A0A089JSP9; -.
DR KEGG; paej:H70737_14325; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_005235_0_0_9; -.
DR Proteomes; UP000029519; Chromosome.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR019800; Glyco_hydro_3_AS.
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:SF10; BETA-GLUCOSIDASE F-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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000029519}.
FT DOMAIN 323..399
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 929 AA; 102064 MW; F1254233AD092AB6 CRC64;
MSTQNVGIPL EGFAEFSRTV AAEGAVLVKN DNQVLPLGEG DNVAIFGRSQ VNYYRSGTGS
GGSVHVTYTT NLLDGLRTKK NFTVNEELAA VYEKWIEQNP FDNGGGAWAA EPWHQKEMSL
SNELVSEARN KSNKAILVIG RTAGEDQDNA DAPGSYQLTN DEQAMLKQVT TYFEQTIVVL
NVSNIIDMNW MNDESYKYPI STVIYSWQGG MEGGNAIADV LSGEVTPSGK LTDTIAYSIN
DYPSTQNYGN EFTNLYQEDI YVGYRYFETF CPDKVQFEFG YGLSYTTFSI EPEEAKLITK
EGESFIEIGV TVTNTGTSFT GKEVVQVYYE APQGKLGKPA KALVSFGKTK VLEPGEAQRL
TVSFSAHSMA SYDDAGVTGH ASAYVLEEGT YRLYVGTSVK QVVAVGVEGK DGYVVEALQV
VEQLQEALAP TESFTRMMPG AQKADGSYEI VYVEVPKRKI SLAERIETNL PETISQTGNK
GYKLRDVYEQ KVSMEAFIAQ LSDEDLAAIV RGEGMSSPLV TPGTASAFGG VSDSLFNLGI
PVACTADGPS GIRMDSGAKA TQVAIGTLLA ATWNADLVEE LYVMEGQELL RNNVDSLLGP
GLNIRRSPLN GRNFEYFSED PLISGVFAAA CTRGILKGGS TATMKHFACN NQEKHRSKVN
AVVSERALRE IYLKGFEISV KQGGSNSIMT SYNPVNGHWA ASNYDLNTTI LRGEWGFKGI
VMTDWWAIMN DVVNGGPADR KFTNWMVRAQ NDLYMVVPNY GSEINGWNDN TIESLENGTL
TRGELQRSAI NICEFIMNAP VFSRKQEIVE TVEFFKANPS LTEEQAQSLS QNPQVKPVVE
GSTSFKVEQA GQYRILVHIM STEPELAQSA CNVSVNDQLM TTIQTNGTEG QWIRQKLVKV
ELEAGLYDMK LEFIKPGLQI DWIEFNKID
//