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Database: UniProt
Entry: A0A0B2BXS8_9SPHN
LinkDB: A0A0B2BXS8_9SPHN
Original site: A0A0B2BXS8_9SPHN 
ID   A0A0B2BXS8_9SPHN        Unreviewed;       808 AA.
AC   A0A0B2BXS8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=PK98_11810 {ECO:0000313|EMBL:KHL24645.1};
OS   Croceibacterium mercuriale.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL24645.1, ECO:0000313|Proteomes:UP000030988};
RN   [1] {ECO:0000313|EMBL:KHL24645.1, ECO:0000313|Proteomes:UP000030988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coronado {ECO:0000313|EMBL:KHL24645.1,
RC   ECO:0000313|Proteomes:UP000030988};
RA   Coil D.A., Eisen J.A.;
RT   "Draft genome sequence of Kirrobacter mercurialis.";
RL   Submitted (NOV-2014) 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   -!- 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:KHL24645.1}.
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DR   EMBL; JTDN01000002; KHL24645.1; -; Genomic_DNA.
DR   RefSeq; WP_039097098.1; NZ_JTDN01000002.1.
DR   AlphaFoldDB; A0A0B2BXS8; -.
DR   STRING; 1572751.PK98_11810; -.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000030988; 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; 2.60.120.430; Galactose-binding lectin; 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   InterPro; IPR041443; Exop_C.
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   PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF18559; Exop_C; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KHL24645.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030988};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..808
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002087225"
FT   DOMAIN          66..389
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          426..639
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          677..796
FT                   /note="ExoP galactose-binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF18559"
FT   REGION          92..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   808 AA;  84599 MW;  503D086E8B7AB680 CRC64;
     MRQAGICSII GATLLASTAM AQDAGPVAGA SASTAHPDLW PQARSRGLVD PATEAFVTEL
     MTRMSLEEKV GQMIQADTSA ITPDDLRRYP LGSILSGGSS PPLGRPDRSP GPDWAATVNA
     FEAVAMEPRT GHTAIPLIFG IDAVHGNNNV VGATLFPHNI ALGATRNLDL TRRIGDATAQ
     ETAAAGIHWA FGPTLAVPQD DRWGRTYEGY SEDPQLVRAF SGAMVEGLQG KPGLTTIQVG
     RVAASAKHFL GDGGTTSGVD QGNTELSEAE LIATHAPGYP PAINGGVMTI MASFNSWNGQ
     KMHGNRSLLT DVLKGRMGFD GFIVGDWNGH AQVAGCTKTD CAASFNAGLD MAMAPDSWQG
     LFDTTLAQVR AGTIPMERVD DAVRRILRVK HRLGLFDTAR PFADRPGVIG APAHRAIARE
     AVRQSLVLLK NDGVLPLRPD AKLLVAGTHA DDIGLQSGGW TLSWQGDGNS NADFPNAQSI
     YAGLAEAVRA GGGSATLSAD GSFTDRPDAA IVVFGEMPYA EGRGDVRTLE FEAGDKQSLA
     LLQRLKAAGI PTVSVFLSGR PLWVNPELNQ SDAFVAGWLP GSEGGGIADV LIAGPDGAPR
     HDFRGRLSFS WPKTAGQFTL NVGQDGYDPL FPYDYGLSYA QGGSVPQLAE EAGVDASLAN
     TGVFFARGRV PGPFALQLDD TVTQGAVDSP LLQEGALQLR WRGAGTARIT GPELALSRET
     NGDTALQLQY RMDRVPAGPV QLTLGNGALD VAGLLVAGGW RSLRVPLHCF APATADAPVT
     IRAAPPFTLS LAEARLVNGP EGAQCPAK
//
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