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Beta-galactosidase BgaA (Beta-gal) (EC 3.2.1.23)

 BGAL_PLASS              Reviewed;         677 AA.
Q9KI47;
03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-FEB-2018, entry version 53.
RecName: Full=Beta-galactosidase BgaA;
Short=Beta-gal {ECO:0000250|UniProtKB:P19668};
EC=3.2.1.23;
Name=bgaA {ECO:0000303|PubMed:10831422};
Planococcus sp. (strain 'SOS Orange').
Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae;
Planococcus.
NCBI_TaxID=128803;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF75984.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, FUNCTION,
CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
SUBSTRATE SPECIFICITY, SUBUNIT, AND BIOTECHNOLOGY.
STRAIN=SOS Orange {ECO:0000312|EMBL:AAF75984.1};
PubMed=10831422; DOI=10.1128/AEM.66.6.2438-2444.2000;
Sheridan P.P., Brenchley J.E.;
"Characterization of a salt-tolerant family 42 beta-galactosidase from
a psychrophilic antarctic Planococcus isolate.";
Appl. Environ. Microbiol. 66:2438-2444(2000).
-!- FUNCTION: Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside
(ONPG), p-nitrophenyl-beta-D-galactopyranoside (PNPG), 5-bromo-4-
chloro-3-indoyl-beta-D-galactosde (X-gal), o-nitrophenyl-beta-D-
fucopyranoside (ONPF) and p-nitrophenyl-beta-D-fucopyranoside
(PNPF) with greatest activity towards ONPG and PNPG and low levels
of activity with ONPF and PNPF. Detectable, but very low levels of
activity towards p-nitrophenyl-beta-lactose (PNPL), p-nitrophenyl-
beta-cellobiose (PNPC), p-nitrophenyl-alpha-galactopyranoside
(PNP-alpha-G), and p-nitrophenyl-beta-xylopyranoside (PNPX).
{ECO:0000269|PubMed:10831422}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
galactose residues in beta-D-galactosides.
{ECO:0000269|PubMed:10831422}.
-!- ENZYME REGULATION: No activity is lost during treatment with 20 or
100 mM EDTA in Z buffer for 3 hours at 0 degrees Celsius, nor is
activity greatly stimulated by the addition of cations. Inhibited
by 1 mM zinc and 1 mM copper, the levels of activity decrease to
10% of the untreated control. Nickel, cobalt and manganese at
concentrations of 10 mM decrease enzyme activity to either 40%
(for nickel and cobalt) or 60% (for manganese) of the activity in
untreated controls. No change in enzyme activity in the presence
of calcium and magnesium at concentrations up to 50 mM. EDTA-
treated enzyme exhibits a slight increase in relative specific
activity when it is assayed in the presence of 50 mM NaCl or 50 mM
KCl, it does not exhibit enhanced activity at concentrations
greater than 250 mM. Maintains between 20 and 40% of activity in
the presence of 4 M NaCl or 4 M KCl, and it is more active in the
presence of KCl than in the presence of NaCl. Retains 50% of
activity in the presence of 3 M KCl or 2.5 M NaCl.
{ECO:0000269|PubMed:10831422}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.4 mM for ONPG (at 1.9 degrees Celsius and at pH 6.5)
{ECO:0000269|PubMed:10831422};
KM=4.5 mM for ONPG (at 10 degrees Celsius and at pH 6.5)
{ECO:0000269|PubMed:10831422};
KM=5.4 mM for ONPG (at 20 degrees Celsius and at pH 6.5)
{ECO:0000269|PubMed:10831422};
KM=5.0 mM for ONPG (at 30 degrees Celsius and at pH 6.5)
{ECO:0000269|PubMed:10831422};
KM=4.9 mM for ONPG (at 39 degrees Celsius and at pH 6.5)
{ECO:0000269|PubMed:10831422};
Vmax=63 umol/min/mg enzyme with ONPG as substrate (at 1.9
degrees Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
Vmax=80 umol/min/mg enzyme with ONPG as substrate (at 10 degrees
Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
Vmax=223 umol/min/mg enzyme with ONPG as substrate (at 20
degrees Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
Vmax=392 umol/min/mg enzyme with ONPG as substrate (at 30
degrees Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
Vmax=467 umol/min/mg enzyme with ONPG as substrate (at 39
degrees Celsius and pH 6.5) {ECO:0000269|PubMed:10831422};
pH dependence:
Optimum pH is 6.5. {ECO:0000269|PubMed:10831422};
Temperature dependence:
Optimum temperature is 42 degrees Celsius. Thermostable at
temperatures at or below the optimal temperature for activity,
but it is rapidly denatured at temperatures above 42 degrees
Celsius. Irreversibly inactivated within 10 minutes at 55
degrees Celsius. Stable during storage at 5 degrees Celsius and
loses no activity during storage for 4 months. Retains 10% of
activity at 0 degrees Celsius. {ECO:0000269|PubMed:10831422};
-!- SUBUNIT: Dimer. {ECO:0000269|PubMed:10831422}.
-!- BIOTECHNOLOGY: Possible reporter enzyme for halotolerant and
halophilic organisms. May also be used in the food industry to
digest plant polysaccharides in high-salt processes.
{ECO:0000269|PubMed:10831422}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
{ECO:0000255}.
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EMBL; AF242542; AAF75984.1; -; Genomic_DNA.
ProteinModelPortal; Q9KI47; -.
SMR; Q9KI47; -.
CAZy; GH42; Glycoside Hydrolase Family 42.
BRENDA; 3.2.1.23; 4880.
GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
Gene3D; 2.60.40.1180; -; 1.
Gene3D; 3.40.50.880; -; 1.
InterPro; IPR013739; Beta_galactosidase_C.
InterPro; IPR013738; Beta_galactosidase_Trimer.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR003476; Glyco_hydro_42.
InterPro; IPR013529; Glyco_hydro_42_N.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR36447; PTHR36447; 1.
Pfam; PF02449; Glyco_hydro_42; 1.
Pfam; PF08533; Glyco_hydro_42C; 1.
Pfam; PF08532; Glyco_hydro_42M; 1.
PIRSF; PIRSF001084; B-galactosidase; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF52317; SSF52317; 1.
1: Evidence at protein level;
Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
Zinc.
CHAIN 1 677 Beta-galactosidase BgaA.
/FTId=PRO_0000407692.
REGION 357 360 Substrate binding.
{ECO:0000250|UniProtKB:O69315}.
ACT_SITE 151 151 Proton donor.
{ECO:0000250|UniProtKB:O69315}.
ACT_SITE 309 309 Nucleophile.
{ECO:0000250|UniProtKB:O69315}.
METAL 116 116 Zinc. {ECO:0000250|UniProtKB:O69315}.
METAL 156 156 Zinc. {ECO:0000250|UniProtKB:O69315}.
METAL 158 158 Zinc. {ECO:0000250|UniProtKB:O69315}.
METAL 161 161 Zinc. {ECO:0000250|UniProtKB:O69315}.
BINDING 112 112 Substrate.
{ECO:0000250|UniProtKB:O69315}.
BINDING 150 150 Substrate.
{ECO:0000250|UniProtKB:O69315}.
BINDING 317 317 Substrate.
{ECO:0000250|UniProtKB:O69315}.
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


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