ID A0A1Y2ZWB1_9GAMM Unreviewed; 737 AA.
AC A0A1Y2ZWB1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BCS42_07505 {ECO:0000313|EMBL:OTE96154.1};
OS Crenothrix sp. D3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=1880899 {ECO:0000313|EMBL:OTE96154.1, ECO:0000313|Proteomes:UP000198219};
RN [1] {ECO:0000313|EMBL:OTE96154.1, ECO:0000313|Proteomes:UP000198219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OTE96154.1};
RA Oswald K., Graf J.S., Littman S., Tienken D., Brand A., Wehrli B.,
RA Albertsen M., Daims H., Wagner M., Kuypers M.M., Schubert C.J., Milucka J.;
RT "Crenothrix are major methane consumers in stratified lakes.";
RL ISME J. 0:0-0(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTE96154.1}.
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; MBQZ01000044; OTE96154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2ZWB1; -.
DR STRING; 1880899.BCS42_07505; -.
DR Proteomes; UP000198219; Unassembled WGS sequence.
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:SF16; LYSOSOMAL 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..737
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012079153"
FT DOMAIN 661..730
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 737 AA; 80523 MW; 2EF7869F25902E16 CRC64;
MKTTALIIAT FVLSSYTVQA DTTIANKVSD LLAQMTLEEK IGQMTQIDFA VIGGDPNADF
PMDTAKLDDA IINHHVGSIL NTPFDKGRSV ETWRKIIQTV QDTAAKSRLK IPVIYGIDAI
HGATFTKNAT LFPQAINMAA TFNPELSGKE GEITAREIKV SGLAWNFYPV MDIGRQPLWA
RLWETYGEDV HLATVMGSAY IKGHQGTDFS APDKAATCLK HFVGYSFPLN GEDRTPAWIS
ERMLREYFLP TFEAGIKAGS PTVMVNSGEV DGIPGHANHH YLTTILREEM GFKGVTVSDW
EDIQRLYTRD KLAASPKEAV KIAVMAGIDM SMVPNDFSFS ELLLELVKSN EVPLARIDEA
VTRILTVKYQ TGLFNPDTTF LPISQFATAE AQQINQQAAH ESIVLAKNAN SVLPLKKSAS
ILVTGPTANL LSILNGGWTM TWNGDNESLY PQGKATVLKA LQQKSTGKIT YIEGSSFDTE
KNIDQVIAEA KNHDYVLLCL GEKTYIETFG NIDSLALEPV QMKLANAVLA TGKPVILLML
GGRPRIITPI ADQAAGVLLG FLPSMEGGVA IADILYGDYN PNGKLPISYP RNTNGITPYD
YKPSEVFKPN TYSPLYPFAH GLSYTTFATS GLTLEKHTIT RSETLNVTVQ VKNTGAVKGK
EVVLLYLNDV AASVTRPNKQ LKAFKKIELN PNQTETVTFT LTPADLSFIG VDLQRIVEAG
DFNVMIGNES ATFTVTE
//