ID   BGH3A_BACO1             Reviewed;         747 AA.
AC   A7LXS8;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Beta-glucosidase BoGH3A;
DE            EC=3.2.1.21;
DE   AltName: Full=Glycosyl hydrolase family protein 3A;
DE            Short=BoGH3A;
DE   Flags: Precursor;
GN   ORFNames=BACOVA_02644;
OS   Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 /
OS   CCUG 4943 / NCTC 11153).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=411476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC
RC   11153;
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides ovatus (ATCC 8483).";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=24463512; DOI=10.1038/nature12907;
RA   Larsbrink J., Rogers T.E., Hemsworth G.R., McKee L.S., Tauzin A.S.,
RA   Spadiut O., Klinter S., Pudlo N.A., Urs K., Koropatkin N.M., Creagh A.L.,
RA   Haynes C.A., Kelly A.G., Cederholm S.N., Davies G.J., Martens E.C.,
RA   Brumer H.;
RT   "A discrete genetic locus confers xyloglucan metabolism in select human gut
RT   Bacteroidetes.";
RL   Nature 506:498-502(2014).
CC   -!- FUNCTION: Catalyzes the hydrolysis of terminal, non-reducing beta-D-
CC       glucosyl residues with release of beta-D-glucose in xyloglucan
CC       degradation, leading to remove the backbone 'G' units.
CC       {ECO:0000269|PubMed:24463512}.
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:0000269|PubMed:24463512};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.49 mM for cellotetraose {ECO:0000269|PubMed:24463512};
CC         KM=0.698 mM for cellohexaose {ECO:0000269|PubMed:24463512};
CC         Note=kcat is 65.0 sec(-1) for cellotetraose. kcat is 0.62 sec(-1) for
CC         cellohexaose.;
CC       pH dependence:
CC         Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512};
CC   -!- PATHWAY: Glucan metabolism; xyloglucan degradation.
CC       {ECO:0000269|PubMed:24463512}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. Note=Periplasmic
CC       localization is predicted by analogy with the archetypal sus locus.
CC       {ECO:0000269|PubMed:24463512}.
CC   -!- MISCELLANEOUS: Gut bacteria supply the human body with energy from
CC       dietary polysaccharides through glycosidases that are absent in the
CC       human genome. Xyloglucans are a ubiquitous family of highly branched
CC       plant cell wall polysaccharides present in the vegetables we consume.
CC       Enzymes involved in xyloglucan degradation mediate the conversion of
CC       otherwise indigestible plant polysaccharides to short-chain fatty acids
CC       (PubMed:24463512). {ECO:0000305|PubMed:24463512}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; AAXF02000049; EDO11435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7LXS8; -.
DR   SMR; A7LXS8; -.
DR   STRING; 411476.BACOVA_02644; -.
DR   EnsemblBacteria; EDO11435; EDO11435; BACOVA_02644.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_4_1_10; -.
DR   SABIO-RK; A7LXS8; -.
DR   UniPathway; UPA01045; -.
DR   Proteomes; UP000005475; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0085030; P:symbiotic process benefiting host; IDA:UniProtKB.
DR   GO; GO:2000899; P:xyloglucan catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 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   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; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Periplasm;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..747
FT                   /note="Beta-glucosidase BoGH3A"
FT                   /id="PRO_0000425892"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   747 AA;  83348 MW;  D719F87E4883B015 CRC64;
     MIIGIMKTFL LTICFLSVQT GMVAIAQDKE QTPVYLDDTQ PIEVRVQDAL NRMTVEEKTR
     LSYAQGKFSS PGCPRLGIPE LWMSDGPHGV RAEINWNDWG YAGWTNDSCT AFPALTCLAA
     SWNPLLAAKY GYAIGEEARY REKDVLLGPG VNIYRTPLNG RNFEYMGEDP YLASELCVPY
     IQGVQKNGVA ACVKHYALNN QELWRGHIDV QLSDRALYEI YLPAFKAAVE RGKAWSIMGA
     YNKVRGTHAT HHKLLNNDIL KGEWNFDGCV ITDWGAAHDT YEAAMYGLDI EMGSYTNGLT
     SESEFGYDDY YLGKSYLKMV REGKIPMEVV NDKAARVLRL IFRTAMNRRK PFGALTSEEH
     YRTAYEIATE GIVLLKNGTG KKQPALLPVP QGKYKRILVV GDNATRNLML GGGSSELKVQ
     KVISSLDGIK AKFGDGVVYA QGYTSGRPMY GRADVIPQVT VDSLRNDAVE KAMNSDLVIF
     VGGLNKNHFQ DCEGGDRLSY ELPFAQNELI EALLKVNKNL VAVIVSGNAV EMPWVKEIPS
     IVQSWYLGSV GGEALADVLS GEVTPSGKLP FSYPVKLEDC PAHFFGEISY PGDSIRQEYK
     EDILVGYRWY DTKKVQPLFP FGYGMSYTTF EYSKPVISAQ TMNTDGSIDV SVKVKNTGKV
     AGKEIIQLYI GDEECSVLRP VKELKDFRKV QLLPNEEKEV KFTIKPEALQ FFDDKQRTWV
     AEPGKFKAYI AASSSDIRGT VTFEYIQ