ID A0A196LDL2_9MICO Unreviewed; 754 AA.
AC A0A196LDL2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=A4X16_11910 {ECO:0000313|EMBL:OAN41207.1};
OS Microbacterium sp. H83.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1827324 {ECO:0000313|EMBL:OAN41207.1, ECO:0000313|Proteomes:UP000078289};
RN [1] {ECO:0000313|EMBL:OAN41207.1, ECO:0000313|Proteomes:UP000078289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H83 {ECO:0000313|EMBL:OAN41207.1,
RC ECO:0000313|Proteomes:UP000078289};
RA Lymperopoulou D., Adams R.I., Lindow S., Coil D.A., Jospin G., Eisen J.A.;
RT "Draft Genome Sequences of Staphylococcus capitis Strain H36, S. capitis
RT Strain H65, S. cohnii Strain H62, S. hominis Strain H69, Mycobacterium
RT iranicum Strain H39, Plantibacter sp. Strain H53, Pseudomonas oryzihabitans
RT Strain H72, and Microbacterium sp. Strain H83, isolated from residential
RT settings.";
RL Submitted (APR-2016) 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:OAN41207.1}.
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DR EMBL; LWCU01000010; OAN41207.1; -; Genomic_DNA.
DR RefSeq; WP_067117554.1; NZ_LWCU01000010.1.
DR AlphaFoldDB; A0A196LDL2; -.
DR STRING; 1827324.A4X16_11910; -.
DR OrthoDB; 3187421at2; -.
DR Proteomes; UP000078289; 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; 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:SF16; LYSOSOMAL 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 672..741
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 754 AA; 80806 MW; 757A63F3B3CF63E2 CRC64;
MTSQTLTDSP TDLDSAPYLD RDLPVAARVA DLLDRMTVEE KVGQMLQLDA RDDLEDHVLR
RHVGSILHTS PERILQANAL TARTRLRIPL LVGEDCIHGH SFWPGATIYP TQLGMAATWN
AELVEKVARA TAIEVAATGI HWTFSPVLCI ARDLRWGRID ETFGEDPFLI GELASAMVRG
YQGDGLDDPT AILATAKHFA GYSETQGGRD ASEADISRRK LRSWFLPPFE RVAREGCRTF
MLGYQTTDGV PITVNDWLLS DVLRGEWGYT GTLITDWDNV GRMVWEQQVQ PDHTHAAAAA
VKAGNDMIMT TPGFFEGALD AVAKGMLDED AFDEAVARIL TLKFELGLFE DPRLPGRRLD
AMVGSAAHAE LNLETARRSL VLLENDGVLP LDATAPLRVA VVGPLADDAQ TQLGDWAGGS
GQAGWLDGQP REMITTVLDG LSGVAGWTVA HARGADILTL EADPRGATFP DGQPRPSVVV
PADADESLIT EAVAAAEASD VVVAVVGDRI ELVGEGRSTA TLELIGGQNA LLDALIATGT
PVVVVLLASK PLVLPASVSR AAAVIWAANP GMQGGRALAE VVTGAVEPSG RLPISFARHV
GQQPTYYNQI RGQHGDRYAD LTQAPAWAFG EGRSYSTVAY ADLSLTSTRL GLDDTVVGAV
TVTNTGTRAV RETVQVYVRD VVTSVSWTDK ELKTFRQIDL APGETRRVEL QLPVAECTIV
DAAGIRLVEP GEFALLVGPS SRDEVLLSAG FTVV
//
