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Database: UniProt
Entry: BGAL_PLASS
LinkDB: BGAL_PLASS
Original site: 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-MAY-2023, entry version 63.
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; Bacillota; 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   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:SF1; BETA-GALACTOSIDASE GANA; 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.
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
//
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