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   25-MAY-2022, entry version 86.
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; Firmicutes; 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 = an alcohol + D-
CC         galactose 6-phosphate; 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:0033920; F:6-phospho-beta-galactosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019512; P:lactose catabolic process via tagatose-6-phosphate; IEA:InterPro.
DR   HAMAP; MF_01574; LacG; 1.
DR   InterPro; IPR005928; 6P-beta-galactosidase.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR01233; lacG; 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"
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