ID A0A0Q7TWY6_9CAUL Unreviewed; 714 AA.
AC A0A0Q7TWY6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ASD21_03880 {ECO:0000313|EMBL:KQY99161.1};
OS Caulobacter sp. Root1455.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1736465 {ECO:0000313|EMBL:KQY99161.1, ECO:0000313|Proteomes:UP000051447};
RN [1] {ECO:0000313|Proteomes:UP000051447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1455 {ECO:0000313|Proteomes:UP000051447};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY99161.1, ECO:0000313|Proteomes:UP000051447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1455 {ECO:0000313|EMBL:KQY99161.1,
RC ECO:0000313|Proteomes:UP000051447};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KQY99161.1}.
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DR EMBL; LMFQ01000012; KQY99161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7TWY6; -.
DR Proteomes; UP000051447; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT DOMAIN 632..701
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 714 AA; 76622 MW; BDC2BE4038049110 CRC64;
MTPEEKAGQL SCYSDMIRPP IGDINPLVNQ RNTQQILADV RAGRIGVLMN GVGVEGALLA
QTAAVEQSRL RIPLLFAADV IHGFKTIYPI PLAEAASFDP ILAERTARAA AVEASSHGNH
WTFAPMVDVA RDQRWGRGAE GSGEDVFLGE VMAQARVRGF QGPNLAAPDS LLSTAKHFAG
YGAVAAGLDY NTVDLSEETL REIHLPPFKA AFDAGCLSVM SAFNDINGVP STANKHLLTD
ILRGEWDFKG VVISDYTADQ ELVAHGYAAD DKDAARLAIL AGVDISMQSG LYSRYLPALV
AEGLVPMATV DNAVRRVLSL KETLGLFDRP FRSIDAKAQA ANTATPAMRA LSREAGGKSI
VLLRNDGGLL PLPTTGRKIA LIGPFAEDRD NILGPWAFFG DQSLGVDLAT GIREAMADPS
QLIVAKGCEV ENTIPGGYEQ AVAAARAADV VLLAVGEGQN MSGEAQSRTE IGLPRVQQQL
AEWVASVGKP TVVLLRHGRA LVLEGAVKAA PAVLATWFLG TETGHAVADV LFGKVNPSAR
LPVSFPHESG QEPFAYNHRT TGRPAPQADD SQEYKARWRT TRNEALYPFG HGLSYTSFAL
SDVKLSTTRL GWNERLYVTA TVTNTGKVAG EHVVQLYIRD RVASRTRPVR ELKRFLKVAL
KPGETREARF SLERAALMFV GDNDQWVAEP GIFDLWVASS AVDGLAASFE LLGA
//
