ID A0A3N1X8Q1_9BURK Unreviewed; 799 AA.
AC A0A3N1X8Q1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=EC845_2058 {ECO:0000313|EMBL:ROR23144.1};
OS Comamonas sp. BIGb0124.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2485130 {ECO:0000313|EMBL:ROR23144.1, ECO:0000313|Proteomes:UP000267274};
RN [1] {ECO:0000313|EMBL:ROR23144.1, ECO:0000313|Proteomes:UP000267274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIGb0124 {ECO:0000313|EMBL:ROR23144.1,
RC ECO:0000313|Proteomes:UP000267274};
RA Samuel B.;
RT "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL Submitted (NOV-2018) 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:ROR23144.1}.
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DR EMBL; RJVF01000009; ROR23144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1X8Q1; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000267274; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000267274};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..50
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 51..799
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018055524"
FT DOMAIN 719..788
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 86257 MW; 6C57B135E8D46828 CRC64;
MQIISGKPSL GRNAQAPTQG TRRAPGLRWR RVALATALAF PLAGLSPAWA QTASPDSSQT
RLETKSAFVA DLIGRMTLDE KIGQLRLISI GSDMPAAKLA DEIAAGRIGA SFNTVTRKDN
RPLQAAAVER SRLKIPVLFA YDIVHGHRTV FPISLGLAST WDMQAVELAA RTAAVEAAAD
GIDMTFAPMV DISRDPRWGR TSEGFGEDPH LVSEAARASV RGFQGMSLAA PDSIGASVKH
FALYGAVEGG RDYNTVDMSP MRMYQDYLPP YRAAVDAGAA GVMVALNSIN GVPATSNTWL
MQDLLRKQWG FKGVTVSDHG AITELVKHGV ARDSREAAKL AIKAGIDLSM ADQVYLQELP
RLVQSGEVSM QEIDNAVREV LGVKYDLGLF SDPFRRIGTA DGDPVDVNAE QRLHRAATRD
VARKSLVLLE NRNGTLPLRK AGTIALVGPL ADSPIDIMGS WSAAGVAKQS VTLRQGLEAA
VRGRARVVYA RGSNVTDDPA IVEYLNFLNW DTPEVVNDKR PAADQIAEAV RAAQQADVVV
AAVGEARGMS HESSSRTSLE LPASQRDLLA ALKATGKPLV LVLMNGRPLA LDWAKKNADA
VLETWYTGTE GGHAISDVLF GDYNPAGKLP VSFARSVGQI PTYYNHLRIG RPFTPGKPGN
YTSQYFEEPN GPLYPFGYGL SYTRFELSDV SLSAPTMARG GRVTASIAVR NAGDRAGETV
VQLYIEDPAA SVARPVKELK DFRKIMLQPG EQQVVRFEID EQKLAFYNAK LEHVAEDGQF
NVQIGLDSQD VKVGTFELR
//
