ID H2CFD7_9LEPT Unreviewed; 442 AA.
AC H2CFD7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=Lepil_3099 {ECO:0000313|EMBL:EHQ07762.1};
OS Leptonema illini DSM 21528.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptonema.
OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ07762.1, ECO:0000313|Proteomes:UP000005737};
RN [1] {ECO:0000313|EMBL:EHQ07762.1, ECO:0000313|Proteomes:UP000005737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ07762.1,
RC ECO:0000313|Proteomes:UP000005737};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL Submitted (OCT-2011) 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; JH597773; EHQ07762.1; -; Genomic_DNA.
DR RefSeq; WP_002773893.1; NZ_JH597773.1.
DR AlphaFoldDB; H2CFD7; -.
DR STRING; 183.GCA_002009735_03091; -.
DR HOGENOM; CLU_001859_1_0_12; -.
DR Proteomes; UP000005737; Unassembled WGS sequence.
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};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000005737}.
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 352
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 405..406
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 442 AA; 50328 MW; 43D8572C52CFEA25 CRC64;
MKRSDFGRDF LWGAASASYQ IEGAYNEDGK GESVWDRFTH TPGKIHDGST GDVACNHYHL
FEKDLDIMKE MGLPLYRFSI GWPRIFPTGS GAKNQKGVDF YHRLIDGCLS RGIEPAVTLY
HWDLPQALED RGGWTSRETY EHFCEYVDFA TKEYGSKIKR WMILNEPFAF TTLGYMLGQH
APGRKGPSNY LPAVHHTALA QGEGGRIAKA NCPNAEVGTT YSCSWIEPAG SFSAQAAARY
DYLMNRMFVE TGLGLGYNTK LLPLLKKLDA FQKEGDDSRM KFDFDFIGIQ NYSREIIRWS
PFIPYVWGSM IPAKKRCPKT TDMGWEIYPD GIYHLLKQFA SYKGVKKIYV TENGAAFPDV
VTGDRVHDAE RTQFIQDYLG AVLRAKNEGV NVQGYIIWSF TDNFEWAEGY RPRFGLVHVD
YETQKRTVKD SGLWFRGFLA GK
//
