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   28-JUN-2023, entry version 68.
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; Deinococcota; Deinococci; Thermales; Thermaceae; 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   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   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
//