ID H8MU66_CORCM Unreviewed; 1499 AA.
AC H8MU66;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=bglX {ECO:0000313|EMBL:AFE08202.1};
GN OrderedLocusNames=COCOR_03977 {ECO:0000313|EMBL:AFE08202.1};
OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS (Myxococcus coralloides).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Corallococcus.
OX NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE08202.1, ECO:0000313|Proteomes:UP000007587};
RN [1] {ECO:0000313|EMBL:AFE08202.1, ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RX PubMed=22582372; DOI=10.1128/JB.00397-12;
RA Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA Sogaard-Andersen L.;
RT "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT coralloides DSM 2259.";
RL J. Bacteriol. 194:3012-3013(2012).
RN [2] {ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT DSM 2259.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003389; AFE08202.1; -; Genomic_DNA.
DR STRING; 1144275.COCOR_03977; -.
DR KEGG; ccx:COCOR_03977; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_250830_0_0_7; -.
DR InParanoid; H8MU66; -.
DR Proteomes; UP000007587; Chromosome.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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 Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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:SF120; BETA-GLUCOSIDASE C; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00754; F5_F8_type_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 SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR PROSITE; PS50022; FA58C_3; 3.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AFE08202.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007587}.
FT DOMAIN 34..176
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 179..314
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1354..1460
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1499 AA; 161000 MW; AFA24123EB8BE9FB CRC64;
MSESLPQLSS RGASPCLHEA PRVWLLQAFT AVLMLVSFLG ASNAHAQTNV ALNKTTYTSS
AEAPFLGQYA VDGDGGTRWA SGFTANEWIT VDLGQTRTIS RVVLTWEAAY ATVYKIQVST
NNTTFTDALT VNTGDGATDD LSLPSGITGR YVRMQGVTRA LPAYGYSLWE FAVYETGGTP
PPTNTDLARN RSATASSVEA DAAGLQPGFA FDGDVNTRWA SAQGVDPQWI RVDLGSSQVV
GKVVLDWEGA YGKTYTIDGS NNDTSWTTLN TVTNGAIGRR EIPVSGTWRY IRMRGTERGT
GYGYSLWSFE VYQNGGTTPP PTQTTNQTIK LNFPELAYAK INVSPAPLSV TPVPEEGNTT
PSVRNPPGPF TYQLTFPPNT TVTLSKNQFS PTQPNTDIRL AVVDYNGVQQ RAQSVTALAV
QGADWNVEIF STGNGPTDPR DPTIIPDPYV APAPLPVAGA FRLAAPGNNA MITATRRPTL
SWATVTGATN YKLYVNLTRN DYDWMAAGNL LDRYTQVASQ TGTSFTFTED LPDRWTYKWY
VVATLSGGST SRSDIGNFSV YLPVVETQAD GVNLINGIRD LNKNGTIEPY EDWHNPISVR
VNDLLGRMTL REKALQMFYD AKTYPEAGFQ MGPLSPTDIP MFQKASAATR LGIPHIDAGD
TIHGYKTSWP TQPALAATRD LDTIYEMGDI QRREQLAIGS RGTLSPLAEV NTKVLYPRTQ
EGNGEDADLA AGITRALIAG LQGGPEVNPS SIWVTTKHWP GQGAGGEAGI TYDGTTIHYH
MRPWHAAIEA GTSGIMPGYA GSWLLGPEGY GAGDNPGILN YLRNQLKYDG VICSDWLPSG
SWVRSATAGS DVMGGATPQA MANFENEVPV ARINDSVRRI LDLKFRLGIF EDPYKQGPAG
TSQWHTADSK AAVRRAAQES MTLLKNDGAL PIRLPAGGRL VIAGPRADDM SCMVTWRSDF
HGTEFGDPTI YAAVKARAEA AGLTVYKDNA PAGVTPDAAI VVVGESYFTH GTEWDKEKPY
LPGDPIGPAH DAKWGDQYGI INSFRSRGIP TTVVLISPRP YVLTNVVPLS NALMLAYRPG
DMGGYAVADV LFGDVLPRGK TPWQLPRGMN QIGTDVENNQ LEKWDLPFDL GATDAERAAI
RQKIATGQPV PPTYGNPLFQ YGAGIQGFGL TDATPPVAFN LLTPSNNLVI TGTRPAFTWA
ASSDPQTGVQ RYEVYLDGGA MPVAITRTPS AALDGLKLAN GVHTWFVKAF NWANGVTQSA
TFTFTLNDTT PPAAFAALSP SAGQAVPGTS TRFIWEQTTD VGAGVAEYVL IVDGTDRGPS
ILRSTPVPAG TNLARGKNAY ATSVEFGSAN DAVDGSLATR WSSVGTATTG DTESITIDLG
AIYSLKRIVL NWEAAYGRRY VLEASLDGST NWTALRTVDT GDGGIDDWTV AGVGRFVRMR
GVQRATAYGY SLWEFEVYGV GTEQTTLNGL STGSHTWRVR AVDGANNTTL SSGPITFTK
//