ID A0A0Q8AKA9_9MICO Unreviewed; 846 AA.
AC A0A0Q8AKA9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ASD56_07425 {ECO:0000313|EMBL:KQZ86320.1};
OS Microbacterium sp. Root166.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736478 {ECO:0000313|EMBL:KQZ86320.1, ECO:0000313|Proteomes:UP000051650};
RN [1] {ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|Proteomes:UP000051650};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ86320.1, ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|EMBL:KQZ86320.1,
RC ECO:0000313|Proteomes:UP000051650};
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:KQZ86320.1}.
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DR EMBL; LMGL01000001; KQZ86320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8AKA9; -.
DR STRING; 1736478.ASD56_07425; -.
DR Proteomes; UP000051650; 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:KQZ86320.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051650}.
FT DOMAIN 660..729
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 846 AA; 89304 MW; A4A1E808526CBA2B CRC64;
MTLEEKAAQT ASPFGTAVDA HQPPALGWGT ATAAIAALNL PPREAAARVN ELQRKHIEDT
RLGIPVLLAE EALLGFKVQG ATTFPDAIAQ AATWDPDLIA EMGAEIGAQM TTLGARMALS
PLADVARDPR WGRVGETYGE DPYLVGATAS AFVRGLQNSN PDAPVIAALK HFVAYGASDG
GRNTEPAQVG DRLLREFYGV PFEMAIRDGG ANGIMPSYND LDGVPVTGSP ELLDDLLRGD
YGFDGLVISD LDAIGQLHTK HGVSASFVAA FADAIRAGVD IDLDNRVSTD RVVEAVQTGL
LSEVELDRAV AAILRAKFRL GLFENPYIDI DSVPETLDSP AARSLARRVA EESIVLLKND
PVDGTPLLPL SSAPGTVAVI GPNADRPLGQ LGHYAYQVLD SMTKRFALAA NPQARLEDVE
ELRGRTGADD ATLLVETVPL VTFLEGIRDR LGDDADVLYE AGCPVERIDR SGIPAAVEAA
RRAEVAVLVV GDQAGINGFG TVGEGLDSAT CELPGVQREL VEAVLDTGTP TIVVLSHARP
YILRWLADRA PAIVSAWLGG EEAGAATAAV LFGDVNPAGR LPIAMLENVG SAPVPYWRTL
QASDSYVDGS AGALFPFGHG LSYSQFEYSD LQLQTPEVGT DGVIRATFTV KNTSERAGDE
VVQVYGRDLV GRTVRRTRVL LGFKRLMLAA GEEQSVLAEI PSEMFALWDR RDGWLVEPGA
VRLFIGGSSA VTPLRGRVEL VGGLHRCAHN RALWSTVTPG ADMPDIAPGE MVGGAPAVAP
LTSESTIGDW LEHPHGRTVL SSALGGADED ALAQAVGLTL DQLVMYSQGA LPADLPATLL
ASVNQH
//
