ID   LACG_STAAB              Reviewed;         470 AA.
AC   Q2YYJ9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=SAB2070c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81759.1; -; Genomic_DNA.
DR   RefSeq; WP_000169224.1; NC_007622.1.
DR   AlphaFoldDB; Q2YYJ9; -.
DR   SMR; Q2YYJ9; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; sab:SAB2070c; -.
DR   HOGENOM; CLU_001859_1_3_9; -.
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   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..470
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_0000260724"
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         430
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         431
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"
FT   BINDING         439
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
SQ   SEQUENCE   470 AA;  54565 MW;  9A5C8E295AB8DF2F CRC64;
     MTKTLPEDFI FGGATAAYQA EGATNTDGKG RVAWDTYLEE NYWYTAEPAS DFYNRYPVDL
     ELSEKFGVNG IRISIAWSRI FPNGYGEVNP KGVEYYHKLF AECHKRHVEP FVTLHHFDTP
     EVLHKDGDFL NRKTIDYFVD YAEYCFKEFP EVKYWTTFNE IGPIGDGQYL VGKFPPGIKY
     DFEKVFQSHH NMMVAHARAV KLFKDGGYQG EIGVVHALPT KYPFDPSNPE DVRAAELEDI
     IHNKFILDAT YLGKYSRETM EGVQHILSVN GGKLNITDED YAILDAAKDL NDFLGINYYM
     SDWMRGYDGE SEITHNATGD KGGSKYQLKG VGQREFDVDV PRTDWDWMIY PQGLYDQIMR
     VVKDYPNYHK IYITENGLGY KDEFIESEKT VHDDARIDYV RQHLNVIADA IKDGANVKGY
     FIWSLMDVFS WSNGYEKRYG LFYVDFETQE RYPKKSAYWY KELAETKEIK
//