BGAL_PLASS
ID BGAL_PLASS Reviewed; 677 AA.
AC Q9KI47;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Beta-galactosidase BgaA;
DE Short=Beta-gal {ECO:0000250|UniProtKB:P19668};
DE EC=3.2.1.23;
GN Name=bgaA {ECO:0000303|PubMed:10831422};
OS Planococcus sp. (strain 'SOS Orange').
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=128803;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF75984.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, SUBUNIT, AND BIOTECHNOLOGY.
RC STRAIN=SOS Orange {ECO:0000312|EMBL:AAF75984.1};
RX PubMed=10831422; DOI=10.1128/aem.66.6.2438-2444.2000;
RA Sheridan P.P., Brenchley J.E.;
RT "Characterization of a salt-tolerant family 42 beta-galactosidase from a
RT psychrophilic antarctic Planococcus isolate.";
RL Appl. Environ. Microbiol. 66:2438-2444(2000).
CC -!- FUNCTION: Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG), p-
CC nitrophenyl-beta-D-galactopyranoside (PNPG), 5-bromo-4-chloro-3-indoyl-
CC beta-D-galactosde (X-gal), o-nitrophenyl-beta-D-fucopyranoside (ONPF)
CC and p-nitrophenyl-beta-D-fucopyranoside (PNPF) with greatest activity
CC towards ONPG and PNPG and low levels of activity with ONPF and PNPF.
CC Detectable, but very low levels of activity towards p-nitrophenyl-beta-
CC lactose (PNPL), p-nitrophenyl-beta-cellobiose (PNPC), p-nitrophenyl-
CC alpha-galactopyranoside (PNP-alpha-G), and p-nitrophenyl-beta-
CC xylopyranoside (PNPX). {ECO:0000269|PubMed:10831422}.
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:10831422};
CC -!- ACTIVITY REGULATION: No activity is lost during treatment with 20 or
CC 100 mM EDTA in Z buffer for 3 hours at 0 degrees Celsius, nor is
CC activity greatly stimulated by the addition of cations. Inhibited by 1
CC mM zinc and 1 mM copper, the levels of activity decrease to 10% of the
CC untreated control. Nickel, cobalt and manganese at concentrations of 10
CC mM decrease enzyme activity to either 40% (for nickel and cobalt) or
CC 60% (for manganese) of the activity in untreated controls. No change in
CC enzyme activity in the presence of calcium and magnesium at
CC concentrations up to 50 mM. EDTA-treated enzyme exhibits a slight
CC increase in relative specific activity when it is assayed in the
CC presence of 50 mM NaCl or 50 mM KCl, it does not exhibit enhanced
CC activity at concentrations greater than 250 mM. Maintains between 20
CC and 40% of activity in the presence of 4 M NaCl or 4 M KCl, and it is
CC more active in the presence of KCl than in the presence of NaCl.
CC Retains 50% of activity in the presence of 3 M KCl or 2.5 M NaCl.
CC {ECO:0000269|PubMed:10831422}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.4 mM for ONPG (at 1.9 degrees Celsius and at pH 6.5)
CC {ECO:0000269|PubMed:10831422};
CC KM=4.5 mM for ONPG (at 10 degrees Celsius and at pH 6.5)
CC {ECO:0000269|PubMed:10831422};
CC KM=5.4 mM for ONPG (at 20 degrees Celsius and at pH 6.5)
CC {ECO:0000269|PubMed:10831422};
CC KM=5.0 mM for ONPG (at 30 degrees Celsius and at pH 6.5)
CC {ECO:0000269|PubMed:10831422};
CC KM=4.9 mM for ONPG (at 39 degrees Celsius and at pH 6.5)
CC {ECO:0000269|PubMed:10831422};
CC Vmax=63 umol/min/mg enzyme with ONPG as substrate (at 1.9 degrees
CC Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
CC Vmax=80 umol/min/mg enzyme with ONPG as substrate (at 10 degrees
CC Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
CC Vmax=223 umol/min/mg enzyme with ONPG as substrate (at 20 degrees
CC Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
CC Vmax=392 umol/min/mg enzyme with ONPG as substrate (at 30 degrees
CC Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
CC Vmax=467 umol/min/mg enzyme with ONPG as substrate (at 39 degrees
CC Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:10831422};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius. Thermostable at
CC temperatures at or below the optimal temperature for activity, but it
CC is rapidly denatured at temperatures above 42 degrees Celsius.
CC Irreversibly inactivated within 10 minutes at 55 degrees Celsius.
CC Stable during storage at 5 degrees Celsius and loses no activity
CC during storage for 4 months. Retains 10% of activity at 0 degrees
CC Celsius. {ECO:0000269|PubMed:10831422};
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:10831422}.
CC -!- BIOTECHNOLOGY: Possible reporter enzyme for halotolerant and halophilic
CC organisms. May also be used in the food industry to digest plant
CC polysaccharides in high-salt processes. {ECO:0000269|PubMed:10831422}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR EMBL; AF242542; AAF75984.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KI47; -.
DR SMR; Q9KI47; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR BRENDA; 3.2.1.23; 4880.
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..677
FT /note="Beta-galactosidase BgaA"
FT /id="PRO_0000407692"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT ACT_SITE 309
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 357..360
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
SQ SEQUENCE 677 AA; 77484 MW; 2A1928DADC945E55 CRC64;
MINDKLPKIW HGGDYNPEQW DSKEIWDEDV RMFKLAGIDV ATLNVFSWAL NQPNEDTYNF
DWLDEKINRL YENGIYTCLA TSTAAHPAWM AKKYPDVLRV DFYGRKRKFG SRHNSCPNSP
TYRKYSERIA ETLAERYKDH PAVLIWHVSN EYGGYCYCDN CQDAFRNWLS DKYGTLEKLN
KAWNTGFWGH TFYEWDEIVA PNMLSEKRED NVSDFQGISL DYRRFQSDRL LDCYKLEYNA
IRKHVPTSIP ITTNLMGTYP MLDYFKWAKE MDVVSWDNYP SIDTPFSYTA MTHDLMRGLK
GGKPFMLMEQ TPSQQNWQPY NSLKRPGVMR LWSYQAIGRG ADTILYFQLR RSVGACEKYH
GAVIEHVGHE HTRVFNEVAQ LGQELNGLSD TLLDARVNAK VAIVFDWENR WATELSSGPS
VSLDYVNEVH KYYDALYKLN VQVDMIGVEE DLSKYDVVIA PVLYMVKEGY AAKVEKFVEN
GGTFLTTFFS GIVNETDIVT LGGYPGELRK VLGIWAEEID ALHPDETNQI VVKGSRGILS
GKYSCNLLFD LIHTEGAEAV AEYGSDFYKG MPVLTVNKFG KGKAWYVASS PDAEFLVDFL
QTVCEEAGVE PLLDVPAGVE TTERVKDGQT YLFVLNHNND EVTIELHGSQ YREVLTDEQV
SGNLVLKEKG VLILAKV
