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 28-JUN-2023, entry version 55. 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; Deinococcota; Deinococci; Thermales; Thermaceae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd03143; A4_beta-galactosidase_middle_domain; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; BETA-GALACTOSIDASE GANA; 1. DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 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; (Trans)glycosidases; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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 //