BGAL_PLASL
ID BGAL_PLASL Reviewed; 676 AA.
AC Q09HN2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Beta-galactosidase BgaP;
DE Short=Beta-gal {ECO:0000250|UniProtKB:P19668};
DE EC=3.2.1.23;
GN Name=bgaP {ECO:0000303|PubMed:17326654};
GN Synonyms=galP {ECO:0000303|PubMed:17326654};
OS Planococcus sp. (strain L4).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=377621;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABI64125.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT,
RP AND BIOTECHNOLOGY.
RC STRAIN=L4 {ECO:0000312|EMBL:ABI64125.1};
RX PubMed=17326654; DOI=10.1021/jf062910r;
RA Hu J.M., Li H., Cao L.X., Wu P.C., Zhang C.T., Sang S.L., Zhang X.Y.,
RA Chen M.J., Lu J.Q., Liu Y.H.;
RT "Molecular cloning and characterization of the gene encoding cold-active
RT beta-galactosidase from a psychrotrophic and halotolerant Planococcus sp.
RT L4.";
RL J. Agric. Food Chem. 55:2217-2224(2007).
CC -!- FUNCTION: Hydrolyzes lactose, o-nitrophenyl-beta-D-galactopyranoside
CC (ONPG), p-nitrophenyl-beta-D-galactopyranoside (PNPG), 5-bromo-4-
CC chloro-3-indolyl-beta-D-galactopyranoside (X-gal), o-nitrophenyl-beta-
CC D-fucopyranoside, p-nitrophenyl-beta-D-mannoside, o-nitrophenyl-beta-D-
CC glucoside, p-nitrophenyl-beta-D-xyloside, p-nitrophenyl-beta-D-
CC cellobioside, p-nitrophenyl-beta-D-arabinoside, p-nitrophenyl-beta-D-
CC lactoside, p-nitrophenyl-beta-D-galacturonide, p-nitrophenyl-beta-D-
CC glucuronide and p-nitrophenyl-alpha-D-galactoside with highest level of
CC activity with ONPG as substrate, intermediate level of activity with
CC PNPG and lower levels of activity with all other chromogenic
CC nitrophenyl analogs. Able to hydrolyze 34% of milk lactose after 60
CC minutes at 5 degrees Celsius. {ECO:0000269|PubMed:17326654}.
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:17326654};
CC -!- ACTIVITY REGULATION: No activity lost during treatment with 100 mM EDTA
CC after 2 hours, and the addition of 1 mM MgCl(2), 1 mM CaCl(2) or 1 mM
CC MnCl(2) has no effect. However, the enzyme activity is inhibited by
CC Zn(2+), Cu(2+), Ni(2+) and Co(2+) to different extents. Addition of
CC Na(+) or K(+) slightly stimulates the enzyme activity at low
CC concentrations and the optimal concentration is 250 mM. A further
CC increase of their concentration of ions above the optimum value results
CC in a decrease in enzyme activity. The enzyme is still active even in
CC the presence of Na(+) or K(+) at a concentration up to 5 M.
CC {ECO:0000269|PubMed:17326654}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 mM for ONPG (at 5 degrees Celsius and at pH 6.8)
CC {ECO:0000269|PubMed:17326654};
CC KM=3.8 mM for ONPG (at 10 degrees Celsius and at pH 6.8)
CC {ECO:0000269|PubMed:17326654};
CC KM=2.9 mM for ONPG (at 20 degrees Celsius and at pH 6.8)
CC {ECO:0000269|PubMed:17326654};
CC KM=20.4 mM for lactose (at 5 degrees Celsius and at pH 6.8)
CC {ECO:0000269|PubMed:17326654};
CC KM=11.2 mM for lactose (at 10 degrees Celsius and at pH 6.8)
CC {ECO:0000269|PubMed:17326654};
CC KM=10.4 mM for lactose (at 20 degrees Celsius and at pH 6.8)
CC {ECO:0000269|PubMed:17326654};
CC pH dependence:
CC Optimum pH is 6.8. Exhibits above 80% of its maximal activity in the
CC pH range 6.0-8.0 using ONPG as substrate at 20 degrees Celsius.
CC {ECO:0000269|PubMed:17326654};
CC Temperature dependence:
CC Optimum temperature is 20 degrees Celsius. Lowering or raising the
CC temperature from 20 degrees Celsius results in reduction of activity
CC when ONPG is used as substrate. Rather stable at or below 25 degrees
CC Celsius, but loses 58% of activity after 30 minutes at 40 degrees
CC Celsius. Loses all activity in only 10 minutes at 45 degrees Celsius.
CC Exhibits 27% of maximal activity even at 0 degrees Celsius, but
CC enzyme activity decreases with a further increase in temperature
CC until it is undetectable above 50 degrees Celsius.
CC {ECO:0000269|PubMed:17326654};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17326654}.
CC -!- BIOTECHNOLOGY: Could conceivably be developed to fulfill the practical
CC requirements to enable its use for lactose removal in milk and dairy
CC products at low temperature or a reporter enzyme for psychrophilic
CC genetic systems. {ECO:0000269|PubMed:17326654}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR EMBL; DQ899950; ABI64125.1; -; Genomic_DNA.
DR AlphaFoldDB; Q09HN2; -.
DR SMR; Q09HN2; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR BRENDA; 3.2.1.23; 15705.
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 Glycosidase; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..676
FT /note="Beta-galactosidase BgaP"
FT /id="PRO_0000407693"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT ACT_SITE 308
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 316
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 356..359
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
SQ SEQUENCE 676 AA; 77312 MW; 6A2354F4544A752E CRC64;
MINDKLPKIW HGGDYNPEQW DSQEIWDEDV RMFKLAGIDV ATLNVFSWAL NQPNEDTYNF
EWLDDKINRL YENGIYTCLA TSTAAHPAWM AKKYPDVLRV DFYGRKRKFG SRHNSCPNSP
TYREYSEKIA DKLAERYKDH PAVLIWHVSN EYGGYCYCDN CQDAFRVWLS DKYGTLEKLN
KAWNTGFWGH TFYEWDEIVA PNMLSEERED NVSDFQGISL DYRRFQSDSL LDCYKLEYNA
IRKHTPNIPI TTNLMGTYPM LDYFKWAKEM DVVSWDNYPA IDTPFSYTAM THDLMRGLKS
GQPFMLMEQT PSQQNWQPYN SLKRPGVMRL WSYQAIGRGA DTILYFQLRR SVGACEKYHG
AVIEHVGHEH TRVFNEVAQI GKEFNQLGDT LLDARVNARV AIVFDWENRW ATELSSGPSV
SLDYVNEVHK YYDALYKLNV QVDMVGVEED LSQYDVVIAP VLYMVKEGYA AKVESFVENG
GTFITTFFSG IVNETDIVTL GGYPGELRKV LGIWAEEIDA LHPDETNEIV VNGSRGSLSG
SYSCNLLFDL IHTEGAQAVA EYGSDFYQGM PVLTVNEFGK GKAWYVASSP DAEFLVDFLQ
TVCEEAGVEP LLSVPEGVET TERVKDGQTY LFVLNHNNKV ESIDLKDSQY QELLSTQQLS
GTVELEAKGV FILAKV
