ID A0A1R1F0Q3_9BACL Unreviewed; 970 AA.
AC A0A1R1F0Q3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:OMF57634.1};
GN ORFNames=BK138_03275 {ECO:0000313|EMBL:OMF57634.1};
OS Paenibacillus rhizosphaerae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=297318 {ECO:0000313|EMBL:OMF57634.1, ECO:0000313|Proteomes:UP000187172};
RN [1] {ECO:0000313|EMBL:OMF57634.1, ECO:0000313|Proteomes:UP000187172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0378 {ECO:0000313|EMBL:OMF57634.1,
RC ECO:0000313|Proteomes:UP000187172};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:OMF57634.1}.
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DR EMBL; MRTP01000001; OMF57634.1; -; Genomic_DNA.
DR RefSeq; WP_076165683.1; NZ_MRTP01000001.1.
DR AlphaFoldDB; A0A1R1F0Q3; -.
DR STRING; 297318.BK138_03275; -.
DR Proteomes; UP000187172; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR Gene3D; 2.60.120.380; -; 1.
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; IPR008999; Actin-crosslinking.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF03422; CBM_6; 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; SM00606; CBD_IV; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF50405; Actin-crosslinking proteins; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 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:UP000187172};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 853..970
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
SQ SEQUENCE 970 AA; 106604 MW; 2ABA1E1A84A57671 CRC64;
MPAQTDYPFQ NTSLPLEERV RDLVSRFTLE EKVELMVQYQ AAVERLGVKA YKHGTEAAHG
MAWLGEATGF PQPIGLGCTW DTELMKRIGS VIGDEARGFY RRNPEVNGLT LWAPTVDLER
DPRWGRTEEA YGEDPILTGK LASALIQGIQ GDHPVYLKAV ATLKHFIANN NEVGRGDASV
SIDPRNMREY YLKAFEIPFK EGGAQSMMTA YNAINGVPAN LSPDVKAIVK DEWGMDGFVV
SDAFDVTGTV RDHGYLDTYK EAVARSVKEG GIDSITDDSA VIKEALREDL REGLLAESDL
DAALTNTFRV RFRLGEFDPE EGNPYAAIDE SVILQPEHAV LSREAARKAM VLLKNDRGLL
PLNADKLNKV AVIGPLAGMV YRDWYSGSLP YAVTPLQGIQ EKLSGAGTNG KTSYSGGTDR
IRLKSKKTGR YVRIQAGEEA ALAATTENAL DASVFEMTDW GWGSHTLISE DNGRYLTTDD
KIVKASSEQI WEWFTKEVFL IHPAEHEQGC VTFSTWNGTP VTVHAESGQL LVGDGQAAET
ANEINVAGAA EVSGEDAPIV HADLFELEIV TDKLQTAKEA AAEADLAVVF VGNHPLINGK
ETIDRPDITL PESQEKLIQE VYTANPNTVV VIVGSYPYAL NWVDANVPSV LYTSHAGQEL
GHALADVLFG DTNPAGRLNM TWYKSVDQLP EFMDYDVIKH GRTYQYFEGE ALYPFGHGLS
YASFRYDGLQ LEKEKLTAGT DQTVRLTCRV TNIGEVAGEE VVQLYGRANQ SRVKRPRKQL
LGFRRVMLQP GETADVSFEV PLDQLAIWDV TRERYCIETG TYMMMAGASS ENLPLTAELV
VDGETIPPRD LTQSTKAINY DDYEGVLIGE CTEGGSAVIV KDQSGWITFR DAKFEDGADT
LRIRAAGAAD AVVEVRLDHP EGLPVGRITL TSGDLQTWQD YSCKLSGIHG SQNVYFILKG
NLAISQFQFA
//
