ID   LACG_STRPC              Reviewed;         468 AA.
AC   Q1JK01;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=MGAS9429_Spy1635;
OS   Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS9429;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000259; ABF32822.1; -; Genomic_DNA.
DR   RefSeq; WP_002988094.1; NC_008021.1.
DR   AlphaFoldDB; Q1JK01; -.
DR   SMR; Q1JK01; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; spk:MGAS9429_Spy1635; -.
DR   HOGENOM; CLU_001859_1_3_9; -.
DR   UniPathway; UPA00542; UER00605.
DR   Proteomes; UP000002433; Chromosome.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
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   NCBIfam; TIGR01233; lacG; 1.
DR   PANTHER; PTHR10353:SF340; 6-PHOSPHO-BETA-GALACTOSIDASE 1; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 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_0000260736"
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;  53811 MW;  C39B4785424AA810 CRC64;
     MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYNRYPVDL
     KLSEEFGVNG IRISIAWSRI FPTGKGEVNP KGVEYYHNLF AECHKRHVEP FVTLHHFDTP
     EALHSNGDFL NRENIEHFVN YAELCFKEFS 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
//