BGH3B_BACO1
ID BGH3B_BACO1 Reviewed; 786 AA.
AC A7LXU3;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Beta-glucosidase BoGH3B;
DE EC=3.2.1.21;
DE AltName: Full=Glycosyl hydrolase family protein 3B;
DE Short=BoGH3B;
DE Flags: Precursor;
GN ORFNames=BACOVA_02659;
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=0.68 mM for cellobiose {ECO:0000269|PubMed:24463512};
CC KM=0.23 mM for cellotetraose {ECO:0000269|PubMed:24463512};
CC KM=0.47 mM for cellohexaose {ECO:0000269|PubMed:24463512};
CC Note=kcat is 1.57 sec(-1) for cellobiose. kcat is 3.99 sec(-1) for
CC cellotetraose. kcat is 4.91 sec(-1) for 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; EDO11450.1; -; Genomic_DNA.
DR RefSeq; WP_004298458.1; NZ_DS264579.1.
DR PDB; 5JP0; X-ray; 2.30 A; A/B=23-786.
DR PDBsum; 5JP0; -.
DR AlphaFoldDB; A7LXU3; -.
DR SMR; A7LXU3; -.
DR STRING; 411476.BACOVA_02659; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblBacteria; EDO11450; EDO11450; BACOVA_02659.
DR GeneID; 29452241; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_10; -.
DR SABIO-RK; A7LXU3; -.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; Periplasm;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..786
FT /note="Beta-glucosidase BoGH3B"
FT /id="PRO_0000425893"
FT ACT_SITE 314
FT /evidence="ECO:0000250"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:5JP0"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:5JP0"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 203..218
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:5JP0"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:5JP0"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:5JP0"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 369..385
FT /evidence="ECO:0007829|PDB:5JP0"
FT TURN 386..390
FT /evidence="ECO:0007829|PDB:5JP0"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 405..418
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 447..451
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 473..481
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 511..516
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 521..528
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 546..556
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:5JP0"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 594..602
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 630..633
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 662..670
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 679..688
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 694..706
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 715..724
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 729..737
FT /evidence="ECO:0007829|PDB:5JP0"
FT HELIX 738..741
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 754..761
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 764..770
FT /evidence="ECO:0007829|PDB:5JP0"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:5JP0"
SQ SEQUENCE 786 AA; 87659 MW; C8464AB824DA537C CRC64;
MKNIKKMVLV SAFAGTCLTP HAQTASPVIP TDPAIETHIR EWLQKMTLEQ KIGQMCEITI
DVVSDLETSR KKGFCLSEAM LDTVIGKYKV GSLLNVPLGV AQKKEKWAEA IKQIQEKSMK
EIGIPCIYGV DQIHGTTYTL DGTMFPQGIN MGATFNRELT RRGAKISAYE TKAGCIPWTF
APVVDLGRDP RWARMWENYG EDCYVNAEMG VSAVKGFQGE DPNRIGEYNV AACMKHYMGY
GVPVSGKDRT PSSISRSDMR EKHFAPFLAA VRQGALSVMV NSGVDNGLPF HANRELLTEW
LKEDLNWDGL IVTDWADINN LCTRDHIAAT KKEAVKIVIN AGIDMSMVPY EVSFCDYLKE
LVEEGEVSME RIDDAVARVL RLKYRLGLFD HPYWDIKKYD KFGSKEFAAV ALQAAEESEV
LLKNDGNILP IAKGKKILLT GPNANSMRCL NGGWSYSWQG HVADEYAQAY HTIYEALCEK
YGKENIIYEP GVTYASYKND NWWEENKPET EKPVAAAAQA DIIITCIGEN SYCETPGNLT
DLTLSENQRN LVKALAATGK PIVLVLNQGR PRIINDIVPL AKAVVNIMLP SNYGGDALAN
LLAGDANFSG KMPFTYPRLI NALATYDYKP CENMGQMGGN YNYDSVMDIQ WPFGFGLSYT
NYKYSNLKVN KPTFNADDEL IFTVDVTNTG KVAGKESVLL FSKDLVASST PDNIRLRNFE
KVSLEPGETK TVTLKLKGSD LAFVGYDGKW RLEKGDFKIK CGDQWMDIVC DQTKVWNTPN
KNTLHK
