BGAL1_LACAC
ID BGAL1_LACAC Reviewed; 667 AA.
AC Q5FJ41; B2LWG4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Beta-galactosidase LacZ;
DE Short=Beta-gal {ECO:0000250|UniProtKB:P19668};
DE EC=3.2.1.23;
GN Name=lacZ {ECO:0000312|EMBL:AAV43283.1}; OrderedLocusNames=LBA1462;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACC38288.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 4356 / DSM 20079 / NBRC 13951 / JCM 1132 / NCIMB 8690;
RX PubMed=19841976; DOI=10.1007/s00284-009-9521-9;
RA Pan Q., Zhu J., Liu L., Cong Y., Hu F., Li J., Yu X.;
RT "Functional identification of a putative beta-galactosidase gene in the
RT special lac gene cluster of Lactobacillus acidophilus.";
RL Curr. Microbiol. 60:172-178(2010).
RN [2] {ECO:0000312|EMBL:AAV43283.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of lactose to its constituent
CC monosaccharides glucose and galactose. {ECO:0000269|PubMed:19841976}.
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:19841976};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.84 mM for o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 37
CC degrees Celsius and pH 6.0) {ECO:0000269|PubMed:19841976};
CC KM=88.9 mM for lactose (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:19841976};
CC pH dependence:
CC Optimum pH is 6.0 for both lactose and ONPG hydrolysis, but lactose
CC hydrolysis activity is more sensitive to changes in pH than ONPG
CC hydrolysis activity. {ECO:0000269|PubMed:19841976};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius for both lactose and ONPG
CC hydrolysis. Retains 16.5% of activity for ONPG hydrolysis and 11.2%
CC of activity for lactose hydrolysis at 4 degrees Celsius. Stable at or
CC below 25 degrees Celsius, but loses 50% of its activity after 1 hour
CC at 37 degrees Celsius and is inactivated after only 40 minutes at 45
CC degrees Celsius. Can hydrolyze 73% of lactose in milk in 30 hours at
CC 10 degrees Celsius. {ECO:0000269|PubMed:19841976};
CC -!- BIOTECHNOLOGY: Has potential for lactose removal from dairy products at
CC refrigerated temperatures. {ECO:0000269|PubMed:19841976}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR EMBL; EU590652; ACC38288.1; -; Genomic_DNA.
DR EMBL; CP000033; AAV43283.1; -; Genomic_DNA.
DR RefSeq; WP_011254470.1; NC_006814.3.
DR RefSeq; YP_194314.1; NC_006814.3.
DR AlphaFoldDB; Q5FJ41; -.
DR SMR; Q5FJ41; -.
DR STRING; 272621.LBA1462; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR PRIDE; Q5FJ41; -.
DR EnsemblBacteria; AAV43283; AAV43283; LBA1462.
DR GeneID; 56943037; -.
DR KEGG; lac:LBA1462; -.
DR PATRIC; fig|272621.13.peg.1384; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_9; -.
DR OMA; SRRHYCF; -.
DR BioCyc; LACI272621:G1G49-1432-MON; -.
DR Proteomes; UP000006381; Chromosome.
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; Reference proteome; Zinc.
FT CHAIN 1..667
FT /note="Beta-galactosidase LacZ"
FT /id="PRO_0000407690"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 153
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 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 355..358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
SQ SEQUENCE 667 AA; 76584 MW; 0034A0EC1C4438D2 CRC64;
MTQLSRFLYG GDYNPDQWPE ETWSKDIHVF KKADINSATI NIFSWALLEP REGKYNFSKL
DKVVQQLSDA NFDIVMGTAT AAMPAWMFKK YPDIARVDYQ DRRHVFGQRH NFCPNSSNYQ
RLAGELVKQL VERYKDNKHI VVWHINNEYG GNCYCENCQN AFRKWLKNKY KTVEGLNKAW
NMNVWSHTIY DWDEIVVPNE LGDVWGIEGS ETIVAGLSID YLRFQSESMQ NLFKMEKKII
KKYDPETPVT TNFHGLPNKM VDYQKWAKGQ DIISYDSYPT YDAPAYKAAF LYDLMRSLKH
QPFMLMESAP SQVNWQPYSP LKRPGQMEAT EFQAVAHGAD TVQFFQLKQA VGGSEKFHSA
VIAHSQRTDT RVFKELADLG KKLKNAGPTI LGSKTKAKVA IVFDWSNFWS YEYVDGITQD
LNYVDSILDY YRQFYERNIP TDIIGVDDDF SNYDLVVAPV LYMVKHGLDK KINDYVENGG
NFVTTYMSGM VNSSDNVYLG GYPGPLKEVT GIWVEESDAV VPGQKIKVLM NGKDYDTGLI
CNLIHPNDAK ILATYASEFY AGTPAVTENQ YGKGRAWYIG TRLEHQGLTQ LFNHIIFETG
VESLVCDSHK LEITKRVTED GKELYFVLNM SNEERTLPSK FTGYEDILTG EKAHKDMKGW
DVQVLRN
