BGAL1_THESP
ID BGAL1_THESP Reviewed; 645 AA.
AC Q8GEA9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 52.
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:15748760};
OS Thermus sp.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus;
OC unclassified Thermus.
OX NCBI_TaxID=275;
RN [1] {ECO:0000312|EMBL:AAN05443.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43815 / IB-21 {ECO:0000312|EMBL:AAN05443.1};
RX PubMed=15748760; DOI=10.1016/j.jbiotec.2004.07.019;
RA Kang S.K., Cho K.K., Ahn J.K., Bok J.D., Kang S.H., Woo J.H., Lee H.G.,
RA You S.K., Choi Y.J.;
RT "Three forms of thermostable lactose-hydrolase from Thermus sp. IB-21:
RT cloning, expression, and enzyme characterization.";
RL J. Biotechnol. 116:337-346(2005).
CC -!- FUNCTION: Hydrolyzes chromogen 5-bromo-4-chloro-3-indolyl-beta-D-
CC galactopyranoside (X-Gal) and p-nitrophenyl-beta-D-galactoside
CC (pNPGal). {ECO:0000269|PubMed:15748760}.
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:15748760};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for pNPGal (at 70 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15748760};
CC KM=42 mM for lactose (at 70 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15748760};
CC Vmax=140 umol/min/mg enzyme with pNPGal as substrate (at 70 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:15748760};
CC Vmax=8.5 umol/min/mg enzyme with lactose as substrate (at 70 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:15748760};
CC pH dependence:
CC Optimum pH is around 5.0-6.0. Retains more than 80% of activity at pH
CC range between 4.5 and 6.5. Retains 10% of activity at pH 4.0.
CC {ECO:0000269|PubMed:15748760};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. Retains 90% of activity
CC even at 95 degrees Celsius. Retains 80% of activity during a 12-hour
CC period of incubation at 70 degrees Celsius. Half-lives at 80 and 90
CC degrees Celsius are 23 and 4.7 hours, respectively.
CC {ECO:0000269|PubMed:15748760};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR EMBL; AY130259; AAN05443.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GEA9; -.
DR SMR; Q8GEA9; -.
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 Glycosidase; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..645
FT /note="Beta-galactosidase BgaA"
FT /id="PRO_0000407695"
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"
SQ SEQUENCE 645 AA; 72714 MW; E1F13D0D598857BE CRC64;
MLGVCYYPEH WPKARWKEDA RRMREAGLSY VRVGEFAWAL LEPEPGRLEW GWLDEALATL
AAEGLKVVLG TPTATPPKWL VDRYPEVLPV DREGRRRRFG GRRHYCFSSP AYREEARRIV
TLLAERYGGL EAVAGFQTDN EYGCHGTVRC YCPRCQEAFR GWLKARYGTI EALNEAWGTA
FWSQRYRNFT EVELPHLTVA EPNPSHLLDY YRFASDQVRA FNRLQVEILR AHAPGKFITH
NFMGFFTDLD AFALAQDLDF ASWDSYPLGF TDLMPLPPEE KLRYARTGHP DVAAFHHDLY
RGVGRGRFWV MEQQPGPVNW APHNPSPTPG MVRLWTWEAL AHGAEVVSYF RWRQAPFAQE
QMHAGLHRPD SAPDQGFFEA KQVAEELAAL ALPPVAQAPV ALVFDYEAAW VYEVQPQGAE
WSYLGLIYLF YSALRRLGLD VDVVPPGASL RGYALTVVPS LPIVRGEALK AFQEAEGIVL
FGPRSGSKTE TFQIPRELPP GPLQALLPLK VVRVESLPPG LLEVAEGPMG RFSLGLWREW
VESPLRPWLA FADGGGALYR EGRYLYLAAW PSPELLGVLL AGLAQEAGLR PVFLPEGLRL
RRRGPWVFAF NYGPEAVEAP APEGARFLLG GKRVGPYDLA VWEEA
