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Database: UniProt
Entry: A0A0Q5M9T7_9MICO
LinkDB: A0A0Q5M9T7_9MICO
Original site: A0A0Q5M9T7_9MICO 
ID   A0A0Q5M9T7_9MICO        Unreviewed;       759 AA.
AC   A0A0Q5M9T7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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=ASF88_02005 {ECO:0000313|EMBL:KQR53657.1};
OS   Leifsonia sp. Leaf336.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736341 {ECO:0000313|EMBL:KQR53657.1, ECO:0000313|Proteomes:UP000050966};
RN   [1] {ECO:0000313|EMBL:KQR53657.1, ECO:0000313|Proteomes:UP000050966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf336 {ECO:0000313|EMBL:KQR53657.1,
RC   ECO:0000313|Proteomes:UP000050966};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR53657.1, ECO:0000313|Proteomes:UP000050966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf336 {ECO:0000313|EMBL:KQR53657.1,
RC   ECO:0000313|Proteomes:UP000050966};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQR53657.1}.
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DR   EMBL; LMOZ01000001; KQR53657.1; -; Genomic_DNA.
DR   RefSeq; WP_055913521.1; NZ_LMOZ01000001.1.
DR   AlphaFoldDB; A0A0Q5M9T7; -.
DR   STRING; 1736341.ASF88_02005; -.
DR   OrthoDB; 3187421at2; -.
DR   Proteomes; UP000050966; 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, ECO:0000313|EMBL:KQR53657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050966}.
FT   DOMAIN          677..746
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   759 AA;  81633 MW;  A9F7795221DC83D1 CRC64;
     MTSILPSTTT EAEQEARLPY QDPSLTTAER VADLLGRMTI EEKVGQMLQL DARDDLRDHV
     LRRHVGSILH TSPERIVEAN RLTGQTRLRI PLLVGEDCIH GHSFWPGATI YPTQLGMAAS
     WDAELIERVA RASAEEVAVT GVHWTFSPVL CIARDLRWGR ISETFGEDPY LIGELASAMV
     RGYQGDGLDD PTAILATAKH FAGYSETQGG RDASEADISR RKLRSWFLPP FERVAREGCR
     TFMLGYQSTD GVPITINDWL LSEVLRGEWG YTGTLITDWD NVGRMVWEQK IQPDHAHAAA
     AAVTAGNDMV MTTPMFFEGA LEAVEKGMLT EDAFDAAVAR ILTLKFDLGL FEDPRLPSPR
     LDEVVGSAAH AELNLEVARR SIVLLENDGT LPLAAAPSAA PLRVALVGPL ADDAQTQLGD
     WAGGSGQAGW LDGQPREMIT TVLDGLQAID GWSVEYARGA DILTLEDDPR GATFPDGQPR
     PRVVVPTPPS TELIAEAVAA AEASDVVVAV VGDRIELVGE GRSTATLELI GGQNALLDAV
     IATGKPVVVV LLASKPLVLP PSAAKAAAVL WAANPGMLGG QAIAEIIAGR VEPSGRLPIS
     FARHVGQQPT YYNQIRGQHG DRYADLTQAP AWAFGQGRSY TTVEYSDLTL ASDALGVDDE
     IVAEVTVSNT GDRPVRETVQ VYVRDLVTSV SWADTELKAY RQVDLAAGET ARVSLRLPVA
     DCTIVDAAGD RHVEAGEFEL LVGASSREVD LLVAGFVVQ
//
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