ID A0A0P0MBL4_9BURK Unreviewed; 451 AA.
AC A0A0P0MBL4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN Name=bglB {ECO:0000313|EMBL:ALK90141.1};
GN ORFNames=L63ED372_02943 {ECO:0000313|EMBL:ALK90141.1};
OS Limnohabitans sp. 63ED37-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK90141.1, ECO:0000313|Proteomes:UP000059510};
RN [1] {ECO:0000313|EMBL:ALK90141.1, ECO:0000313|Proteomes:UP000059510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK90141.1,
RC ECO:0000313|Proteomes:UP000059510};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-2015) 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,
CC ECO:0000256|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR EMBL; CP011774; ALK90141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0MBL4; -.
DR STRING; 1678128.L63ED372_02943; -.
DR KEGG; lih:L63ED372_02943; -.
DR PATRIC; fig|1678128.3.peg.2947; -.
DR Proteomes; UP000059510; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR03356; BGL; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:ALK90141.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:ALK90141.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000059510}.
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 414..415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 451 AA; 50374 MW; 08DBE1453D37B538 CRC64;
MLCGAETFIK MTYPTPSRQH FPDDFIWGVA TSSFQIEGAH LADGKGPSVW DTFCEVKGKI
ADGSNGHVAC EHYQRWPEDV QLIADLGVNA YRFSMSWPRV QPDGQGAWNE AGFAFYDRLI
DALSARGIAL HLTLNHWDLP QALQDQGGWA NRETCAHFTR YATEVARRFG SRLASICTHN
EPWVIAILGY EQGIFAPGIQ SRSQAMQAVH HLLLSHGMAC QAMRGLGLTT PMGIVLNLSP
IYPASQSPED LAKAKLDDGL ILRLYMDALY RGSYPQDVIS HLAEDAPQVK SGDMATIAQP
LDFLGVNYYT RNFSSSGNPW DVASTGNQVT DMGWEVYPQG LTELLCRLHQ DYQPKLLLVT
ENGAAFKDEY KDGVINDTQR LDYVRDHIAA THAAHQQGVP VGGYFAWSLM DNFEWASGYA
KRFGLVHVNF ETQQRTLKNS ALWYQQFLSE K
//
