ID   LACG_STRPM              Reviewed;         468 AA.
AC   Q48RC8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   02-SEP-2026, entry version 107.
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};
GN   OrderedLocusNames=M28_Spy1622;
OS   Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=319701;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS6180;
RX   PubMed=16088825; DOI=10.1086/430618;
RA   Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA   Lefebvre R.B., Musser J.M.;
RT   "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT   potential new insights into puerperal sepsis and bacterial disease
RT   specificity.";
RL   J. Infect. Dis. 192:760-770(2005).
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; CP000056; AAX72732.1; -; Genomic_DNA.
DR   RefSeq; WP_011285166.1; NC_007296.2.
DR   AlphaFoldDB; Q48RC8; -.
DR   SMR; Q48RC8; -.
DR   KEGG; spb:M28_Spy1622; -.
DR   HOGENOM; CLU_001859_1_3_9; -.
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..468
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_0000260739"
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         428
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         429
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         435
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         437
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
SQ   SEQUENCE   468 AA;  53846 MW;  76134ECAE5476CF7 CRC64;
     MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYNRYPVDL
     KLSEEFGVNG IRISIAWSRI FPTGKGEVNP KGVEYYHNLF AECHKRHVEP FVTLHHFDTP
     EALHSDGDFL NRENIEHFVN YAEFCFKEFS EVNYWTTFNE IGPIGDGQYL VGKFPPGIQY
     DLAKVFQSHH NMMVSHARAV KLFKDSGYSG EIGVVHALPT KYPFDANNPD DVRAAELEDI
     IHNKFILDAT YLGKYSDKTM EGVNHILEVN GGELDLREED FAALDAAKDL NDFLGINYYM
     SDWMQAFDGE TEIIHNGKGE KGSSKYQIKG VGRRKAPVDV PKTDWDWIIF PQGLYDQIMR
     VKADYPNYKK IYITENGLGY KDEFVDNTVY DDGRIDYVKK HLEVISDAIS DGANVKGYFM
     WSLMDVFSWS NGYEKRYGLF YVDFETQERY PKKSAYWYKK VAETQVIE
//