BGAC_BIFAA
ID BGAC_BIFAA Reviewed; 1049 AA.
AC A1A3T0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Beta-galactosidase BgaC {ECO:0000303|PubMed:33427933};
DE Short=Beta-gal {ECO:0000305};
DE EC=3.2.1.23 {ECO:0000269|PubMed:33427933};
DE AltName: Full=Lactase {ECO:0000305};
GN Name=bgaC {ECO:0000303|PubMed:33427933};
GN OrderedLocusNames=BAD_1582 {ECO:0000312|EMBL:BAF40363.1};
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RX PubMed=33427933; DOI=10.1007/s00253-020-11084-y;
RA Mulualem D.M., Agbavwe C., Ogilvie L.A., Jones B.V., Kilcoyne M.,
RA O'Byrne C., Boyd A.;
RT "Metagenomic identification, purification and characterisation of the
RT Bifidobacterium adolescentis BgaC beta-galactosidase.";
RL Appl. Microbiol. Biotechnol. 105:1063-1078(2021).
CC -!- FUNCTION: Catalyzes efficient hydrolysis of lactose. Also exhibits
CC transglycosylation activity to produce oligosaccharides at low
CC concentrations of glucose. In vitro, acts on the synthetic chromogenic
CC substrate ortho-nitrophenyl-beta-D-galactopyranoside (ONPG). Acts
CC exclusively on terminal beta-linked Gal residues.
CC {ECO:0000269|PubMed:33427933}.
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:33427933};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:33427933};
CC Note=Mg(2+) enhances the activity by 30%, followed by Ca(2+) and then
CC Zn(2+). {ECO:0000269|PubMed:33427933};
CC -!- ACTIVITY REGULATION: Activity is inhibited by EDTA. Activity is
CC abolished by Cu(2+) and shows 59% reduction in the presence of Mn(2+)
CC (PubMed:33427933). Lactose acts as a competitive inhibitor
CC (PubMed:33427933). {ECO:0000269|PubMed:33427933}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 mM for lactose {ECO:0000269|PubMed:33427933};
CC KM=2.5 mM for ONPG {ECO:0000269|PubMed:33427933};
CC Vmax=22 umol/min/mg enzyme with lactose as substrate
CC {ECO:0000269|PubMed:33427933};
CC Vmax=107 umol/min/mg enzyme with ONPG as substrate
CC {ECO:0000269|PubMed:33427933};
CC pH dependence:
CC Optimum pH is 7.0 with ONPG as substrate. Retains 60% of its activity
CC between pH 6.0 and 8.0. {ECO:0000269|PubMed:33427933};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius with ONPG as substrate.
CC Retains 60% of its activity between 20 and 45 degrees Celsius.
CC {ECO:0000269|PubMed:33427933};
CC -!- BIOTECHNOLOGY: Possesses the industrially desirable properties of high
CC substrate affinity for lactose and low product inhibition by galactose,
CC and is an ideal candidate for dairy industry applications and prebiotic
CC manufacture. {ECO:0000269|PubMed:33427933}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; AP009256; BAF40363.1; -; Genomic_DNA.
DR RefSeq; WP_011743877.1; NC_008618.1.
DR SMR; A1A3T0; -.
DR STRING; 1680.BADO_1688; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; BAF40363; BAF40363; BAD_1582.
DR KEGG; bad:BAD_1582; -.
DR HOGENOM; CLU_002346_0_2_11; -.
DR OMA; HPEYTIT; -.
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:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF16353; DUF4981; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF49303; SSF49303; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..1049
FT /note="Beta-galactosidase BgaC"
FT /id="PRO_0000453260"
FT ACT_SITE 483
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00722"
FT ACT_SITE 557
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00722"
FT BINDING 430
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00722"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00722"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00722"
FT SITE 371
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00722"
FT SITE 405
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00722"
SQ SEQUENCE 1049 AA; 116448 MW; 44D9307C3E31C39D CRC64;
MADTAELAIV HATTASASWL TDPTVFAANR KPAHSSHRYV IGETREPKQS LDGEWKVRIE
QARNVDVESA PFAAVDFEDG DFGAIEVPGH LQMAGYLKNK YVNIQYPWDG HEDPQAPNIP
ENNHVAIYRR RFALDAQLAR TLENDGTVSL TFHGAATAIY VWLDGTFVGY GEDGFTPSEF
DVTEALRNGN GNAADSPEAE HTLTVACYEY SSASWLEDQD FWRLHGLFRT VELAAQPHTH
VETVQLEADY TAADTAGTAD TAELNAALTL RNPADAMTIE STLRDGDGNV VWESTQACNG
EIALNSGKMT NIAPWSAESP TLYTLTVRVV GHDGAIIETV TQKIGFRTFR IENGIMTING
KRIVFKGADR HEFDAKRGRA ITREDMLSDV VFCKRHNINA IRTSHYPNQE YWYDLCDEYG
LYLIDETNME THGTWVANNV ERPEDGIPGS RPEWEGACVD RINSMMRRDY NHPSVLIWSL
GNESSAGEVF RAMYRHAHTI DPNRPVHYEG SVHMREFEDV TDIESRMYAH ADEIERYLND
GSPAHTDGPK KPYISCEYMH AMGNSCGNMD EYTALERYPM YQGGFIWDFI DQAIETKLPD
GTTRMCYGGD FGDRPSDYEF SGDGLLFADR TPSPKAQEVK QLYANVKIAV SVDEARITND
NLFVSTGDYR FVLRILADGK PVWSTTRRFD VAAGESASFE VDWPVDDYRS NAEELVLEVS
QQLGNACDWA PAGYELAFGQ CVVAGAKTTA DAVDAAGAPA DGTVTLGRWN AGVRGQGREA
LFSRTQGGMV SYTFGEREFV LRRPSITTFR PLTDNDRGAG HAFERAAWAV AGKYARCVDC
AIANRGENAV EATYTYELAI PQRTKVTVRY VADTAGLVSL DVEYPGEKNG DLPTIPAFGI
EWALPVEYAN LRFYGAGPEE TYADRRHAKL GVWSTTAGDD CAPYLLPQET GNHEDVRWAE
ITDDSGHGVR VKRGAGAKPF AMSLLPYSST MLEEALHQDE LPKPRHMFLR LLAAQMGVGG
DDSWMSPVHE QYQLPADQPL SLNVQLKLF
