ID E4T124_PALPW Unreviewed; 747 AA.
AC E4T124;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN OrderedLocusNames=Palpr_0243 {ECO:0000313|EMBL:ADQ78405.1};
OS Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=694427 {ECO:0000313|EMBL:ADQ78405.1, ECO:0000313|Proteomes:UP000008718};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB4;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Paludibacter propionicigenes DSM 17365.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ78405.1, ECO:0000313|Proteomes:UP000008718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17365 / JCM 13257 / WB4
RC {ECO:0000313|Proteomes:UP000008718};
RX PubMed=21475585; DOI=10.4056/sigs.1503846;
RA Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Paludibacter propionicigenes type strain
RT (WB4).";
RL Stand. Genomic Sci. 4:36-44(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002345; ADQ78405.1; -; Genomic_DNA.
DR RefSeq; WP_013443774.1; NC_014734.1.
DR AlphaFoldDB; E4T124; -.
DR STRING; 694427.Palpr_0243; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR GeneID; 78489869; -.
DR KEGG; ppn:Palpr_0243; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_10; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000008718; Chromosome.
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:SF121; PERIPLASMIC 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:ADQ78405.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008718};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..747
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003189301"
FT DOMAIN 666..735
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 747 AA; 82951 MW; 4DC44D6FE6D38A45 CRC64;
MKKHVLLLLF TLICLTTLGQ SKSNPAAQAD LLIRQMTLDE KIGQLNQYTS DRNATGKITA
DGDKANQIRQ GKVGSMLNVI GVEETRKLQE LALQSRLKIP MIFGLDVIHG FRTTFPIPLG
ETATWDLELM EKTAHAAATE AAAYGIHWTF APMVDISRDP RWGRVMEGAG EDTYLGCLVA
KARVNGFQGN GLGNIDAIMA CAKHFAAYGA GVGGRDYNSV DMSLRQLNET YLPPFKAAAE
ANVATFMNSF NDINGIPATA NKYIQRDKLK KEWNYKGFVV SDWGSIGEMV AHGYAKNSYD
AAMKAIIAGS DMDMESRCYK DNLKQLVLDK KIDIKLIDEA VKRILIKKFE LGLFEDPFRF
CNQERENKQT NNLANRELAR EAGKKSIVLL KNDNLSTGKP LLPLSKQIKK VALIGPLFKA
TTANHGFWSV AFPDDSSRII SQYQGIKNKL DKSSEILYSH GCNINDNDKS GFEEAVATAK
SADVVILSLG EAANMSGEAK SRSNLHLPGV QEELLKEIHK TGKPIVLLIN AGRPLIFNWA
GDNIPSILYT WWLGTEAGNS IADVLFGDYN PAAKLPMSFP RTEGQIPVYY NHYSTGRPAK
DENDKNYVSA YIDLQNSPRY PFGYGLSYTK FDIDNLKLSS TELSNQKNKL TVTVDLTNSG
NYDGEEVVQL YIRDLFGCVV RPVKELKGFQ KVMLKKGETR QITFTLTPED LKFFNNEIEY
INEAGDYELF VGSSSDASLK ANFKLIL
//
