ID A0A0Q4CQQ9_9SPHN Unreviewed; 724 AA.
AC A0A0Q4CQQ9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KQM27492.1};
GN ORFNames=ASE58_10480 {ECO:0000313|EMBL:KQM27492.1};
OS Sphingomonas sp. Leaf9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM27492.1, ECO:0000313|Proteomes:UP000051210};
RN [1] {ECO:0000313|EMBL:KQM27492.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM27492.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM27492.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM27492.1,
RC ECO:0000313|Proteomes:UP000051210};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:KQM27492.1}.
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DR EMBL; LMKC01000003; KQM27492.1; -; Genomic_DNA.
DR RefSeq; WP_055821138.1; NZ_LMKC01000003.1.
DR AlphaFoldDB; A0A0Q4CQQ9; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000051210; 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; IPR019800; Glyco_hydro_3_AS.
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; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT DOMAIN 632..699
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"
SQ SEQUENCE 724 AA; 75975 MW; 665B95F89E10F1F7 CRC64;
MPMPAAAQTA PVATGPWMDE RQPTEARVAA LLGVMTAEEK MTLIFGQFAT DFPPKQFTAP
AGAREGSAGY VPGIPRLGIP AQWQADAGIG VASQGGAKRK RERTALPSGL ATAATWNPDL
ARRGGAMIGA EAYASGFNVL LGGSVNLTRE PRNGRNFEYA GEDPLLAGTM AGAQIAGIQS
QHVISTMKHF ALNDQETDRN AGNAVIDPKA AHLSDLLAFE IALERGDPGA VMCAYNRVNG
PFSCENPWLL TKVLRSDWGF KGFVMSDWGA THSTEAASAA GLDQQSGYPF DVKPFFGEDM
RRAIAEGRVP PARIDAMVGR ILYAMLRHGL FDHPVTAAPF DLPADMLARN GAVSRADAAE
AIVLLKNSGN VLPLAASAKR ILVIGGHADK GVLAGGGSSL VYPKGGNAVP GLQPAFWPGP
VMYYPSSPLE ALRRRLPGAT IDFVDGTDRA AAAAAAAQAD LAIVFATQWA GEAFDVSLTL
ADNQDALIDA VAGANRRTVV VLENGGPVLT PWAPRVAGIL TAWYPGTEGG EAIADVLTGR
VNPSGHLPMT FPATLDQLPH PQPPVKGEFR YTEGATVGYK WFDAKGLTPA FAFGHGLSYT
DFRYSDLTLT AKNGTIEARF KVANIGRVAG KAVAQLYAAA PGWEAPRRLA GFAKVDLAPR
QGRTVSIAVD PRSVSDYDVA GSCWRPTTGR IGFTLGGSSA DRAAQADLTL PAAALKGARL
CPAF
//