ID LACG_STAA3 Reviewed; 470 AA. AC Q2FEU3; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 99. 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=SAUSA300_2149; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000255; ABD21770.1; -; Genomic_DNA. DR RefSeq; WP_000169220.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FEU3; -. DR SMR; Q2FEU3; -. DR KEGG; saa:SAUSA300_2149; -. DR HOGENOM; CLU_001859_1_3_9; -. DR OMA; DPSWPIC; -. DR UniPathway; UPA00542; UER00605. DR Proteomes; UP000001939; 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..470 FT /note="6-phospho-beta-galactosidase" FT /id="PRO_0000260726" 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; 54550 MW; 9A50A44B5ABFE74F CRC64; MTKTLPEDFI FGGATAAYQA EGATNTDGKG RVAWDTYLEE NYWYTAEPAS DFYNRYPVDL ELSEKFGVNG IRISIAWSRI FPNGYGEVNP KGVEYYHKLF AECHKRHVEP FVTLHHFDTP EVLHKDGDFL NRKTIDYFVD YAEYCFKEFP EVKYWTTFNE IGPIGDGQYL VGKFPPGIKY DFEKVFQSHH NMMVAHARAV KLFKDGGYKG EIGVVHALPT KYPFDPSNPE DVRAAELEDI IHNKFILDAT YLGKYSRETM EGVQHILSVN GGKLNITDED YAILDAAKDL NDFLGINYYM SDWMRGYDGE SEITHNATGD KGGSKYQLKG VGQREFDVDV PRTDWDWMIY PQGLYDQIMR VVKDYPNYHK IYITENGLGY KDEFIESEKT VHDDARIDYV RQHLNVIADA IIDGANVKGY FIWSLMDVFS WSNGYEKRYG LFYVDFETQE RYPKKSAYWY KELAETKEIK //