ID Q2G7L4_NOVAD Unreviewed; 640 AA.
AC Q2G7L4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN OrderedLocusNames=Saro_1719 {ECO:0000313|EMBL:ABD26159.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD26159.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) 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; CP000248; ABD26159.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2G7L4; -.
DR STRING; 279238.Saro_1719; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR KEGG; nar:Saro_1719; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_8_2_5; -.
DR Proteomes; UP000009134; 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 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:SF120; BETA-GLUCOSIDASE C; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 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:ABD26159.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT DOMAIN 91..427
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 500..639
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT REGION 605..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 67530 MW; 1129E7A5FED386FE CRC64;
MGGLKISAPM VLLAGVGAVA LGASASARPA FRDLNHNGRL DPYENVALPV ERRLDDLLKR
MTLEEKVALM LHGTLQAEGG RGIGVGNAYD TALAQELLAR GVNSFITRIA PEPRAFATQN
NAIQRLAEAT RLGIPATIST DPRNHFQVVV GASSDASGFS KWPETLGMAA IGDEKLVERF
GRLVAAEYRA VGIQMALSPQ ADLYTEPRWP RGNATFGSDP ATVSRLAGAY VRGFQGGADG
LVRSGVATVV KHWVGYGAEP EGFDGHNYYG RIARLDNESF AQHVAAFEGA LAAKSAGVMP
TYVIAEGVSI DGKPLPQVGA GFSKPLIEGL LRGTHKFGGI VISDWGITNT CPEQCSNPTA
EKPQGFAIAM PWGVEGLSEE DRYALGANAG IDQFGGVDNP GPLLAAVRAG KVSPARVDQA
ARRVLRLKFE LGLFDDPYVD VEKAAQIVGN KATQAEADAA QRAAQVLLLN RNALLPLAPG
RKVWLSGVDA SAARAAGLVV VDTAEQAEVA IVRVATPHEV LHPHHFFGSR QNEGRLDFRA
GDEATRTIAA AAARIPTVVA VDLDRPAVLT EVKDKATALF GLFGASDAVL LDLVTGKARP
AGKLPFELPS SAKAVEDQHP GRPDDSANPL FRRGDGLTYP
//