ID LACG_STAES Reviewed; 470 AA. AC Q8CNF8; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 118. 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=SE_1781; OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12228 / FDA PCI 1200; RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). 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; AE015929; AAO05422.1; -; Genomic_DNA. DR RefSeq; NP_765336.1; NC_004461.1. DR RefSeq; WP_001832731.1; NZ_WBME01000007.1. DR AlphaFoldDB; Q8CNF8; -. DR SMR; Q8CNF8; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR GeneID; 50018115; -. DR KEGG; sep:SE_1781; -. DR PATRIC; fig|176280.10.peg.1738; -. DR eggNOG; COG2723; Bacteria. DR HOGENOM; CLU_001859_1_3_9; -. DR OrthoDB; 9765195at2; -. DR UniPathway; UPA00542; UER00605. DR Proteomes; UP000001411; 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_0000063891" 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; 54836 MW; E81C610AB95A77EE CRC64; MTKKLPDDFI FGGATAAYQA EGATQTDGKG RVAWDTYLEE NYWYTAEPAS DFYNRYPVDL ELSERFGVNG IRISIAWSRI FPKGYGEVNQ KGVEYYHNLF KECHKRHVEP FVTLHHFDTP EVLHKDGDFL NRKTIDYFVD YAEFCFKEFP EVKYWTTFNE IGPIGDGQYL VGKFPPGIKY DFEKVFQSHH NMMVAHARAV KLFKDENYKG EIGVVHALPT KYPYDPSNPE DVRAAELEDI IHNKFILDAT YLGKYSRETM EGVQHILSVN GGQLEISDED YKILDEAKDL NDFLGINYYM SDWMRGFEGE SEITHNATGD KGGSKYQLKG VGQREFDVDV PRTDWDWMIY PQGLYDQIMR VVKDYPNYHK IYITENGLGY KDVFDEKEKT VHDDARIDYI KQHLSVIADA IADGANVKGY FLWSLMDVFS WSNGYEKRYG LFYVDFETQE RFPKKSAYWY KELAESKEIK //