ID   LACG_LACAI              Reviewed;         473 AA.
AC   P50977;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 98.
DE   RecName: Full=6-phospho-beta-galactosidase {ECO:0000255|HAMAP-Rule:MF_01574};
DE            EC=3.2.1.85 {ECO:0000255|HAMAP-Rule:MF_01574};
DE   AltName: Full=Beta-D-phosphogalactoside galactohydrolase {ECO:0000255|HAMAP-Rule:MF_01574};
DE            Short=PGALase {ECO:0000255|HAMAP-Rule:MF_01574};
DE   AltName: Full=P-beta-Gal {ECO:0000255|HAMAP-Rule:MF_01574};
DE            Short=PBG {ECO:0000255|HAMAP-Rule:MF_01574};
GN   Name=lacG {ECO:0000255|HAMAP-Rule:MF_01574}; Synonyms=pbg;
OS   Lactobacillus acidophilus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LTF42;
RA   Kanatani K., Oshimura M.;
RT   "Isolation and structural analysis of the phospho-beta-galactosidase gene
RT   from Lactobacillus acidophilus.";
RL   J. Ferment. Bioeng. 78:123-129(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-phospho-beta-D-galactoside + H2O = D-galactose 6-phosphate
CC         + an alcohol; Xref=Rhea:RHEA:24568, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:58534, ChEBI:CHEBI:91004; EC=3.2.1.85;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01574};
CC   -!- PATHWAY: Carbohydrate metabolism; lactose degradation; D-galactose 6-
CC       phosphate and beta-D-glucose from lactose 6-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01574}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01574}.
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DR   EMBL; D37882; BAA07122.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50977; -.
DR   SMR; P50977; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   UniPathway; UPA00542; UER00605.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0033920; F:6-phospho-beta-galactosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:TreeGrafter.
DR   GO; GO:0019512; P:lactose catabolic process via tagatose-6-phosphate; IEA:InterPro.
DR   FunFam; 3.20.20.80:FF:000004; Beta-glucosidase 6-phospho-beta-glucosidase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   HAMAP; MF_01574; LacG; 1.
DR   InterPro; IPR005928; 6P-beta-galactosidase.
DR   InterPro; IPR033132; GH_1_N_CS.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   NCBIfam; TIGR01233; lacG; 1.
DR   NCBIfam; NF010036; PRK13511.1; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; LP05116P; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..473
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_0000063881"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         19
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         116
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         159
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         160
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         297
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         433
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         434
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         440
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         442
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
SQ   SEQUENCE   473 AA;  54009 MW;  A7D17EADEC19246A CRC64;
     MTKTLPKDFI FGGATAAYQA EGATKTDGKG RVAWDKFLEE NFWYKGDPAS DFYHNYVEDL
     ELAEKFGGNV IRISIAWSRI FPNGDGEVKP NGVDFYHKLF AECDARHVEP FVTLHHFDTP
     EGLHEDGDFL THEKMDDFVE YADYCFKEFP EVKYWITINE IRSVAVDQYI IGNFPPADTF
     GFDKMFQTHH NQMVGHARAV KLFKHDGSKG EIGIVHALQT NYPFNESNPA DIGAAELEDL
     LDNKFLVDGT FVGKYPQETM EAVKDILAAN HGGEFNIEDE FKAIDAAKDV QDFVGVDYYL
     SEWMRAYDGK SEITHNGTGD KGTSKVQVKG VGEEKLPDGI ETTDWDWLIY PQGLYDKIMR
     VKNDYPNIHK VYITENGIGF KDTVPDNEET DKTVHDDARI DYVKQHLEVI ADAIADGANV
     KGYFIWSLMD VFTWTNGYTK RYGLFYVDFD TQDRYPSKTA DWFKNLAETH IIE
//