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Database: UniProt
Entry: A0A1I2BHT9_9BACT
LinkDB: A0A1I2BHT9_9BACT
Original site: A0A1I2BHT9_9BACT 
ID   A0A1I2BHT9_9BACT        Unreviewed;       750 AA.
AC   A0A1I2BHT9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=SAMN05216283_101411 {ECO:0000313|EMBL:SFE55388.1};
OS   Sunxiuqinia elliptica.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Sunxiuqinia.
OX   NCBI_TaxID=655355 {ECO:0000313|EMBL:SFE55388.1, ECO:0000313|Proteomes:UP000198964};
RN   [1] {ECO:0000313|EMBL:SFE55388.1, ECO:0000313|Proteomes:UP000198964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9156 {ECO:0000313|EMBL:SFE55388.1,
RC   ECO:0000313|Proteomes:UP000198964};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; FONW01000001; SFE55388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2BHT9; -.
DR   STRING; 655355.SAMN05216283_101411; -.
DR   Proteomes; UP000198964; 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; IPR019800; Glyco_hydro_3_AS.
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:SF121; PERIPLASMIC 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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198964};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..750
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011727286"
FT   DOMAIN          670..738
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   750 AA;  81275 MW;  6D6F398A0653779E CRC64;
     MKTTLLILVG LLLCMGANAT VSPKKDEQVE RKIKELIAQM TLEEKLGQMS QFDPGQLGGA
     ESAKQAIRDG KVGSILNLVG ASRVNELQKV AVEESRLGIP LIIGRDVIHG YRTIMPIPLG
     MAASWNAELA EQAMGVAAAE AASEGIHWTF APMIDVSRDP RWGRIAESCG EDTYLTSVMA
     KAMVKGFQGE DLTDSRTIAA CAKHFVGYGA AEGGRDYNTT LIPEVQLRND YLPPFKAAVD
     AGVATFMSAF NDLNGVPASG NEFTLKQILR QEWGYEGMVV SDWASIAEMI PHGYAANQKE
     AAEKALNAGV DMEMASNCYV ENVQALLDEG KIEMATIDSY VANILRLKFS LGLFDQPYTD
     ESLAAKTILS ERHLEIAKEA ASESFVLLQN KNELLPLSKS ISSIAVIGPL ADSPHDQMGT
     WVFDGNKENS VTPLTALKEK LGAAKINFAK GLEISRTKST EGFAEAVEAA KKSDVVVLFL
     GEESILSGEA HSLANLNLQG SQTQLLEAVQ ATGKPVVMVV MAGRQLTIER ELKLADAVLY
     AWHPGTMGGP ALADMLFGEA VPSGKLPVTF PKTVGQIPIY YNHKNTGRPA DYQQWTDINK
     IPAEATQHSL GNTSHYLDAG FEPLFPFGYG LSYSSFDYSN LELSSNTMGV DGAIDVSVTL
     KNTGKYEAAE VVQLYIRDRF GSVTRPVRQL KGYKKVTLKP GESQQVSINL KANELAFFNG
     KDYVIEAGDF DVWMGTNAQE GLHAEFSIDK
//
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