ID A0A097EJ80_9SPHN Unreviewed; 743 AA.
AC A0A097EJ80;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-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=MC45_16035 {ECO:0000313|EMBL:AIT07626.1};
OS Sphingomonas taxi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT07626.1, ECO:0000313|Proteomes:UP000033200};
RN [1] {ECO:0000313|EMBL:AIT07626.1, ECO:0000313|Proteomes:UP000033200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT07626.1,
RC ECO:0000313|Proteomes:UP000033200};
RA Zhou Y., Ma T., Liu T.;
RT "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT RASTools.";
RL Submitted (SEP-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};
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DR EMBL; CP009571; AIT07626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097EJ80; -.
DR STRING; 1549858.MC45_16035; -.
DR KEGG; stax:MC45_16035; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_5; -.
DR Proteomes; UP000033200; Chromosome.
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; 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.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000033200};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..743
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001929846"
FT DOMAIN 662..731
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 587..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 77802 MW; AD5DEEA6AFBEA773 CRC64;
MVSRRSVLLG MSMLPAWPAL AREAQDRIDD LIGRMTIEEK AGQLSCFSDT IRPLGRPTNP
GEAARDAAAM LMAIRAGQIG MLFNGHGVAG ARKAQRAALQ SRLGIPLVFA ADVIHGYETI
FPIPLGEAAA FDAALSERIA RAVASEATAG GLHWTFAPMV DVARDQRWGR VAEGAGEDVH
LGCVLAAARV RGFQGNDLSA DDALCATPKH FAGYGAVGGG MEYGAVDVSP ATLRAVHVPP
FAAAFAAGAG AVMASFTDVN GIPATANRPL LTGLLRDELA FRGPCVSDYQ ADLELIAHGA
ASDEADAARR AILAGTDVSM QSGLYNAHLP ALVAAGRVPM ARVDEAVRRV LGLKMRLGLF
DRPFRSLDRA AERTRIGTLA TRALAREAAT RAVVLLRNDG DLLPLSSATK RIALIGPFGD
DPAQLDGPWS FAGYRRTGID LATTLRGRIT APTRLIVEPG SGIEAPIPGG IERAVAAARG
ADIVLLAIGE GGDMSGEANS RTSITIPVAQ QALADAVAAT DRPIVVLLRH GRALALQGAV
AAAPAILATW FLGCETGPAL ADILFGDVEP TGRLPVSFPF ATGQEPWSYD RLPTGRPPPA
EPQPQGGTGR WRDAPDAACY AFGHGLGYTR FALETVTAPP VLADASDVVV TVRNIGARRG
THLVQLYVRQ RVASLARPVR QLKRFAHVTL DAGESRAVAL PLGPADLAIV DGRGTRRIEP
GDVDIWIASS SADPGLHAVT RLV
//