BGAL2_THESP
ID BGAL2_THESP Reviewed; 645 AA.
AC O54315;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Beta-galactosidase BgaA;
DE Short=Beta-gal {ECO:0000250|UniProtKB:O69315};
DE EC=3.2.1.23;
GN Name=bgaA {ECO:0000303|PubMed:9603833};
OS Thermus sp.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus;
OC unclassified Thermus.
OX NCBI_TaxID=275;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB07810.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 27737 / T2 {ECO:0000312|EMBL:CAB07810.1};
RX PubMed=9603833; DOI=10.1128/aem.64.6.2187-2191.1998;
RA Vian A., Carrascosa A.V., Garcia J.L., Cortes E.;
RT "Structure of the beta-galactosidase gene from Thermus sp. strain T2:
RT expression in Escherichia coli and purification in a single step of an
RT active fusion protein.";
RL Appl. Environ. Microbiol. 64:2187-2191(1998).
CC -!- FUNCTION: Hydrolyzes chromogen 5-bromo-4-chloro-3-indolyl-beta-D-
CC galactopyranoside (X-gal), o-nitrophenyl-beta-D-galactopyranoside
CC (ONPG) and lactose. {ECO:0000269|PubMed:9603833}.
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:9603833};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for ONPG (at 70 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:9603833};
CC Vmax=191000 nmol/min/mg enzyme with ONPG as substrate (at 70 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:9603833};
CC Vmax=13000 nmol/min/mg enzyme with lactose as substrate (at 70
CC degrees Celsius and pH 7.0) {ECO:0000269|PubMed:9603833};
CC Vmax=435000 nmol/min/mg enzyme with ONPG as substrate (at 70 degrees
CC Celsius and pH 5.0) {ECO:0000269|PubMed:9603833};
CC pH dependence:
CC Optimum pH is 5.0 with ONPG as substrate.
CC {ECO:0000269|PubMed:9603833};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius with ONPG as substrate.
CC Stable for several months at 4 or -20 degrees Celsius in the presence
CC of 10% glycerol. Activity increases continuously from 30 to 90
CC degrees Celsius and drops dramatically at higher temperatures.
CC Retains 50% of its initial activity after 1 hour incubation at 70
CC degrees Celsius. Retains 90% and 50% of activity after 30 minutes of
CC incubation at 70 and 80 degrees Celsius, respectively. The residual
CC activity of the enzyme decreases to an undetectable level after
CC heating for 30 minutes at 90 degrees Celsius. The enzyme still
CC maintains significant activity at 30 degrees Celsius.
CC {ECO:0000269|PubMed:9603833};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR EMBL; Z93773; CAB07810.1; -; Genomic_DNA.
DR AlphaFoldDB; O54315; -.
DR SMR; O54315; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR013739; Beta_galactosidase_C.
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; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; PTHR36447; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 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 Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..645
FT /note="Beta-galactosidase BgaA"
FT /id="PRO_0000407696"
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT ACT_SITE 312
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 360..363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT CONFLICT 2..3
FT /note="LG -> ST (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 73221 MW; 7A2AC9EAB6BAC944 CRC64;
MLGVCYYPEH WPEERWEEDF KAMRALGLRY VRLGEFAWSA LEPTPGALRW GWLDRVLDLA
QKEGLAVVLG TPTATPPKWL VDRYPEILPV DREGRRRNFG GRRHYCFSSP AYREETARIV
ALLAERYGRH PAVVGFQVDN EFGCHGTVRC YCPNCREAFR GWLRAKYGTI DALNAAWGTV
FWSQTYRDFG EVELPHLTVA EANPSHLLDY YRFASDQVRA YNRFQVDLLR DNAPGRFITH
NFMGFFTDLD PFALAEDLDF AAWDSYPLGF TDLMPLPQEE KVQWARTGHP DVAAFHHDLY
RGVGRGRFWV MEQQPGPVNW APHNPSPAPG MVRLWTWEAI AHGAEVVSYF RWRQAPFAQE
QMQAGFNRPD FQPEVAFFEV QRVAEELSAL PLPPAGCAPV ALVYDSEAAW VFEIQPQGAE
WKYLTLVFSF YSVFRRLGLE VDIFKPGAEL GGYGLVVVPS LPIVRKEALE ALSQADGLVI
VGPRSGSKTE KFQIPPEIPP GALQALLPLK VVRVESLPPG LLEEAEGPWG RFAFGVWREW
VETDLPPLLR FTDGGGILFR RGRYLYLAAW PSPELLFALC QSLAEEAGLH PRFLPEGLRL
RRRGPLVFAF NYGPEVVEAP APPGVRFLLG DRRIPPHDLA VWEET
