ID A0A0Q8M5B5_9CAUL Unreviewed; 738 AA.
AC A0A0Q8M5B5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KRB44479.1};
GN ORFNames=ASE02_02240 {ECO:0000313|EMBL:KRB44479.1};
OS Phenylobacterium sp. Root700.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1736591 {ECO:0000313|EMBL:KRB44479.1, ECO:0000313|Proteomes:UP000051042};
RN [1] {ECO:0000313|EMBL:KRB44479.1, ECO:0000313|Proteomes:UP000051042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root700 {ECO:0000313|EMBL:KRB44479.1,
RC ECO:0000313|Proteomes:UP000051042};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB44479.1, ECO:0000313|Proteomes:UP000051042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root700 {ECO:0000313|EMBL:KRB44479.1,
RC ECO:0000313|Proteomes:UP000051042};
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:KRB44479.1}.
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DR EMBL; LMHT01000022; KRB44479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8M5B5; -.
DR STRING; 1736591.ASE02_02240; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000051042; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..738
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006349229"
FT DOMAIN 655..720
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 738 AA; 77203 MW; BAEE529C0179953F CRC64;
MLERRWRRRG VELVAVTAMA WTASAAAQDR TQAPAQRAAA TVGQMTLDEK LSLVHGYFGA
SLKGAPPPMN ATPPKEALGG AGYVPGVSRL GVPALQESDA SLGVANGGNM RPGDQATALP
SGLATASTWN PQLAHDGGAM IGTEAHAKGF NVLLAGGVNL ARDPRNGRNF EYLGEDTLLA
GVMAGESIAG IQSRHVISTV KHFAINDQET GRMTLSSDID EKAMRETDLL AFEIAIERGK
PGAVMCSYNR INGEYGCEND FLLNKVLKGD WAYPGWVMSD WGGVHSTVKA AMGGLDQESA
HTFDKQDFFG APLKAAVESG QVPMARLDDM AGRILHSMYA VGVVEHPPVK RDIDKAAHAA
VAQKVAEEGA VLLKNEGGLL PLAAQAKSIA VIGAHADVGV LSGAGSSQVI SYGGSALELP
GKGAFGGLFK IVYHASSPMK AIAAAAPGAK VSFSGGQDIA AAVAAAKQAE VAIVFAEQWQ
TEIQDAPNLS LPDGQDALIA AVAAANPRTI VVLQTGNPVL MPWLSNVGAV LEVWYPGQRG
GEAIANILFG KVNPSGKLPI SFPQSEAQLP RPKIPGSELK FVLFGGNDPL FSVPYPEGSE
VGYRGFEARG QKPLFPFGHG LSYTHFTYGG LKVAGGETLK VSFTLTNAGA REGMEVAQVY
ATPPGQQRRL IGWKKVALKP GETRKVEVSA DPRLLAEYDV KAPGWRVSAG DYAVAVGASS
ADLRLNGASR VTATLLKP
//