ID U5ND43_9BURK Unreviewed; 1301 AA.
AC U5ND43;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=Cenrod_2092 {ECO:0000313|EMBL:AGX88163.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX88163.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX88163.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX88163.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
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};
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DR EMBL; CP004885; AGX88163.1; -; Genomic_DNA.
DR STRING; 946483.Cenrod_2092; -.
DR KEGG; cbx:Cenrod_2092; -.
DR PATRIC; fig|946483.4.peg.2107; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_9_1_4; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000017184; 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; 2.60.120.430; Galactose-binding lectin; 3.
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 InterPro; IPR041443; Exop_C.
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 PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF18559; Exop_C; 3.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000017184};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1301
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004662909"
FT DOMAIN 79..402
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 440..666
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT DOMAIN 727..880
FT /note="ExoP galactose-binding-like"
FT /evidence="ECO:0000259|Pfam:PF18559"
FT DOMAIN 958..1083
FT /note="ExoP galactose-binding-like"
FT /evidence="ECO:0000259|Pfam:PF18559"
FT DOMAIN 1160..1287
FT /note="ExoP galactose-binding-like"
FT /evidence="ECO:0000259|Pfam:PF18559"
SQ SEQUENCE 1301 AA; 139007 MW; 23CD6C165C647AB0 CRC64;
MRTFFPYSRN AVALAAALTV AIMAGCGGGS STDDPSTDDP GTTTGLSYTP LTDWPTLVSD
IQKNATIEQE VKALVDSMTL AEKVGQMVQP ETISITPAEV GQYFIGSVLS GGGTWPDGNK
TASAADWVQR ADDYWAASQT TRLKVPVMWG IDAVHGHNNV YKATIFPHNI GLGAANDPAL
IQRIGEATAM QLAATGTDWN FGPTVAVARD DRWGRTYESY SEDPKIVNDY ASRMVKGLQG
DFTRTTSPNV IATAKHFIGD GGTDLGDNEG VNKSSKIDMI NIHGWGYYSA IDAGVQTVMA
SFSSWVSDGI TVGKMHGSKE MLTDVLKTKM GFDGLVIGDW NGHAQVTGCT NTSCAAAINA
GVDIIMVPAD WKAFLTDTIT KVESNTIPIA RINDAVTRIL RVKKRAGLFA ALRPTQRANA
GVEAKLLHRD LAREAVRKSL VLLKNNGEVL PLQRGKRILV VGKSADSIPN QMGGWSLTWQ
GTSNTNADFP NADSILAGIR EAAGTFNVTY SKDATGVDPT QFDAVIAVLG EEPYAESQGD
IDPMADTGTL EHALRAPDDL AVLNKVSGKG KPVVTVFIAG RPLVVNKELN RSNAFVMAWL
PGSEGKGVAD VLFRKADGSV NVGFTGKLSF SWPKSECQSP LNVGSDRTTY ATDNTPLFAY
GYGLRYGDNK TVANQTEPTR NYGCGQSAPV VVPPATEELA FFKNGSAQTD FTLALGSSVG
TDNWYKPVGT QSSLTVAPIQ IETGKQITAA GDAFQITVSP NNGEGQVYIQ YTQNGTHGGS
NDLSSYAADG ANTALVFDTI VHTAPSGEVE MRIADAWPKI ATMSAKNLFK SMQVGTKYTA
KVPLTCFTKK DAFSFKKVAT PFLLGVANAS FSASFANIRW VPGAADDADA SCESVTPSGS
TTTAELALLN QTVPSPYGMY LGSATAPTSG ASGANTWRQP ISAVLPAMSV VTDPTNVSAK
KVTWTGTELG QVYIQRSDEK PTGDVTQYQN KDTALVFDAQ VYQAPQGVVT MQLDSQWPNR
ALWTATQMFK NIGTTKKTVK VPLSCFVNTT ADQSTGFHYD KALTLFFVGT DKAFQASFSN
IRWVVGAAKD VDAVQCDGTF PSVSPTTPEL ALLNQTVPSP YGMYLGSATA PTSGASGENW
WRQPISAVLP AMSVVTDPTD ASAKKVTWTG TELGQVYIQR SDEKPTGDVT QYQNKDTALV
FDAQVYQAPQ GVVTMQLDSQ WPNRALWTAT QMFQNLGTTK KTVKVPLSCF VNTTDDHSTG
FHYDKALTLF FVGTNKQFQA SFSNIRWVVG AAKDADAVLC N
//
