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Database: UniProt
Entry: A0A0Q5CUP4_9BURK
LinkDB: A0A0Q5CUP4_9BURK
Original site: A0A0Q5CUP4_9BURK 
ID   A0A0Q5CUP4_9BURK        Unreviewed;       734 AA.
AC   A0A0Q5CUP4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KQQ36312.1};
GN   ORFNames=ASF61_07325 {ECO:0000313|EMBL:KQQ36312.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ36312.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ36312.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ36312.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ36312.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ36312.1};
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}.
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:KQQ36312.1}.
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DR   EMBL; LMNW01000023; KQQ36312.1; -; Genomic_DNA.
DR   RefSeq; WP_056156568.1; NZ_LMNW01000023.1.
DR   AlphaFoldDB; A0A0Q5CUP4; -.
DR   STRING; 1736266.ASF61_07325; -.
DR   OrthoDB; 8864425at2; -.
DR   Proteomes; UP000051032; 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; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          643..712
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   734 AA;  77995 MW;  97F408FC4574526D CRC64;
     MMTGAAHAAA DAKRPWLDAA QSPDARAEQL VKAMTLDEKI QTVFGYFSTD FESKQYTAPK
     DGRKDSAGFV PGIERLGLPS QWQTDAGMGV ATQAASKSPL ERTSLPSGLS TAATWDRKLA
     YAGGHMIGSE ARQSGFNIML AGSVNLMREP RNGRNFEYGG EDPLLAGVMV GEQIRGIQAN
     NVVSTLKHFA FNDQETNRFH INVKIDDAAG RMSDLLALQL AMEVGDPGSV MCAYNRVNGP
     YACESDYLLN EVLKKDWGFK GYVMSDWGAT HSTIPAAIAG LDQQSGHPFD KSAYFNDALK
     EAVVNGHVPQ SRLDDMVKRI TRTMFAHGLA EHPVKAATTK DAGIDYATNG KISQAGAEDG
     IVLLKNSHDI LPLAATVRTI AIIGGHSDVG VMSGGGSAQV YPVGLSPVPN EGPQFFPGPM
     VYHRSSPMQE LASRTKAKLS YADGKDVKAA AKLAAASDLV IVFGNQWTAE SIDAPDLNLP
     NKQDDLIAAV AKANGKTVVV LQTGGPVVMP WLNNVAAVLE AWYPGSNGGA AIARVLTGEV
     NPSGRLPATF PASVSQLPRP KLDGDAVTKD ENILNSLTTN YNIEGAAVGY KWFDLKGHKP
     LFPFGYGLSY TTFAMSDLAA AKRDKGIEVT FNVTNTGKRD GKAVGQVYIA PAKGGWEAPK
     RLGGWDKLAV KAGETGKATV KVDPRLLAMY DSASKTWKIA PGEYVVTLAE SAGAKPAATV
     KVSLDAQTVD IHGK
//
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