BGAL_BIFAA
ID BGAL_BIFAA Reviewed; 700 AA.
AC A1A399; Q5J883;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Beta-galactosidase BgaB;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Beta-Gal II;
GN Name=bgaB; Synonyms=bgaLII; OrderedLocusNames=BAD_1401;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16; 20-29; 455-463
RP AND 535-546, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RX PubMed=15480628; DOI=10.1007/s00253-004-1745-9;
RA Hinz S.W., van den Brock L.A., Beldman G., Vincken J.P., Voragen A.G.;
RT "beta-galactosidase from Bifidobacterium adolescentis DSM20083 prefers
RT beta(1,4)-galactosides over lactose.";
RL Appl. Microbiol. Biotechnol. 66:276-284(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RX PubMed=10742215; DOI=10.1128/aem.66.4.1379-1384.2000;
RA Van Laere K.M., Abee T., Schols H.A., Beldman G., Voragen A.G.;
RT "Characterization of a novel beta-galactosidase from Bifidobacterium
RT adolescentis DSM 20083 active towards transgalactooligosaccharides.";
RL Appl. Environ. Microbiol. 66:1379-1384(2000).
CC -!- FUNCTION: Involved in the hydrolysis of transgalactooligosaccharides
CC (TOS). Highly active towards Gal(beta1-4)Gal and Gal(beta1-4)-Gal-
CC containing oligosaccharides. Low activity towards Gal(beta1-3)Gal,
CC lactose and Gal(beta1-3)GalOMe. No activity towards Gal(beta1-6)Gal,
CC Gal(beta1-4)Man, Gal(alpha1-4)Gal, Gal(alpha1-3)Gal(beta1-4)Gal,
CC lactulose, 3'fucosyllactose, lacto-N-fucopentaose I, lacto-N-
CC fucopentaose II, cellobiose, maltose or sucrose. No transglycosylation
CC activity is found at high substrate concentrations (100 mg/ml) and only
CC low transglycosylation activity at lower substrate concentrations (10
CC mg/ml). {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628};
CC -!- ACTIVITY REGULATION: Inhibited by high substrate concentrations (100
CC mg/ml). No effect on activity with various EDTA concentrations (0-1
CC mM). 20-fold higher activity when cells grown on TOS than when cells
CC grown on galactose, glucose and lactose. {ECO:0000269|PubMed:10742215,
CC ECO:0000269|PubMed:15480628}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 mM for Gal(beta1-4)Gal (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628};
CC KM=2.2 mM for p-nitrophenyl-beta-D-galactopyranoside (PNPG) (at 40
CC degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215,
CC ECO:0000269|PubMed:15480628};
CC KM=2.2 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Glcp (at 40
CC degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215,
CC ECO:0000269|PubMed:15480628};
CC KM=4.0 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-beta-D-Galp-
CC (1->4)-D-Glcp (at 40 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628};
CC KM=3.7 mM for beta-D-Galp-(1->4)-D-Galp (at 40 degrees Celsius and pH
CC 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628};
CC KM=6.4 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Galp (at 40
CC degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215,
CC ECO:0000269|PubMed:15480628};
CC KM=5.2 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-beta-D-Galp-
CC (1->4)-D-Galp (at 40 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628};
CC Vmax=1.129 umol/min/mg enzyme with Gal(beta1-4)Gal as substrate (at
CC 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215,
CC ECO:0000269|PubMed:15480628};
CC pH dependence:
CC Optimum is pH 6.0 using PNPG or TOS as substrate. Not active below pH
CC 5. {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius using PNPG as substrate
CC (PubMed:15480628). Optimum temperature is 35 degrees Celsius using
CC TOS as substrate (PubMed:10742215). Stable at 40 degrees Celsius.
CC Half-life time at 50 degrees Celsius is 10 minutes.
CC {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628};
CC -!- SUBUNIT: Trimer (PubMed:15480628). Tetramer (PubMed:10742215).
CC {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF40182.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY359872; AAR24113.1; -; Genomic_DNA.
DR EMBL; AP009256; BAF40182.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041777416.1; NC_008618.1.
DR PDB; 5VYM; X-ray; 2.46 A; A/B=409-638.
DR PDBsum; 5VYM; -.
DR AlphaFoldDB; A1A399; -.
DR SMR; A1A399; -.
DR STRING; 1680.BADO_1629; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR DNASU; 4557550; -.
DR EnsemblBacteria; BAF40182; BAF40182; BAD_1401.
DR KEGG; bad:BAD_1401; -.
DR HOGENOM; CLU_012430_1_1_11; -.
DR Proteomes; UP000008702; Chromosome.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; PTHR36447; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15480628"
FT CHAIN 2..700
FT /note="Beta-galactosidase BgaB"
FT /id="PRO_0000407683"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 368..371
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 213..230
FT /note="IPRFMGADSMVNPGQKLD -> HPTVHGRRLRWSTPARSST (in Ref.
FT 1; AAR24113)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="N -> T (in Ref. 1; AAR24113)"
FT /evidence="ECO:0000305"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:5VYM"
FT HELIX 419..425
FT /evidence="ECO:0007829|PDB:5VYM"
FT HELIX 437..450
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 468..474
FT /evidence="ECO:0007829|PDB:5VYM"
FT HELIX 480..491
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:5VYM"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:5VYM"
FT HELIX 523..528
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 564..569
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 580..587
FT /evidence="ECO:0007829|PDB:5VYM"
FT HELIX 588..592
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 599..606
FT /evidence="ECO:0007829|PDB:5VYM"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:5VYM"
FT HELIX 620..630
FT /evidence="ECO:0007829|PDB:5VYM"
SQ SEQUENCE 700 AA; 78025 MW; 9EDB064761188A52 CRC64;
MSARRNFEWP ELLTADGRGI AFGGDYNPDQ WSEDIWDDDI RLMKQAGVNT VALAIFSWDR
IQPTEDRWDF GWLDRIIDKL GNAGIVVDLA SATATAPLWL YESHPEVLPR DKYGHPVNAG
SRQSWSPTSP VFKEYALTLC RKLAERYGTN PYVTAWHMGN EYGWNNREDY SDNALEAFRA
WCRRKYGTID ALNQAWGTTF WGQEMNGFDE VLIPRFMGAD SMVNPGQKLD FERFGNDMLL
DFYKAERDAI AEICPDKPFT TNFMVSTDQC CMDYAAWAKE VNFVSNDHYF HEGESHLDEL
ACSDALMDSL ALGKPWYVME HSTSAVQWKP LNTRKRKGET VRDSLAHVAM GADAINFFQW
RASAFGAEAF HSAMVPHAGE DTKLFRQVCE LGASLHTLAD AGVQGTELAH SDTAILFSAE
SEWATRSQTL PSMKLNHWHD VRDWYRAFLD AGSRADIVPL AYDWSSYKTV VLPTVLILSA
ADTQRLADFA AAGGRVVVGY ATGLIDEHFH TWLGGYPGAG DGLLRSMLGV RGEEFNILGA
EAEGEPGEIR LSSADDSAAL DGTTTRLWQN DVNVTGEHAQ VLATYAGEEA DEWELDGTAA
VTRNPYGSGE AYFVGCDLDV ADLTKLVRAY LAASSQENAD VLHTVRASAD ATFDFYLPRG
KKTVELQGIE GEPVILFQTD REEKPGSYTV RRNGVLVVRR
