ID LACG_STRSV Reviewed; 468 AA. AC A3CPH0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 04-NOV-2026, entry version 111. 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=SSA_1692; OS Streptococcus sanguinis (strain SK36). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=388919; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK36; RX PubMed=17277061; DOI=10.1128/jb.01808-06; RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P., RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D., RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.; RT "Genome of the opportunistic pathogen Streptococcus sanguinis."; RL J. Bacteriol. 189:3166-3175(2007). 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}. 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; CP000387; ABN45075.1; -; Genomic_DNA. DR RefSeq; WP_002923665.1; NC_009009.1. DR AlphaFoldDB; A3CPH0; -. DR SMR; A3CPH0; -. DR STRING; 388919.SSA_1692; -. DR KEGG; ssa:SSA_1692; -. DR PATRIC; fig|388919.9.peg.1604; -. DR eggNOG; COG2723; Bacteria. DR HOGENOM; CLU_001859_1_3_9; -. DR OMA; AACDFMG; -. DR OrthoDB; 9765195at2; -. DR UniPathway; UPA00542; UER00605. DR Proteomes; UP000002148; Chromosome. 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:0005990; P:lactose catabolic process; IEA:UniProtKB-UniRule. 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; Reference proteome. FT CHAIN 1..468 FT /note="6-phospho-beta-galactosidase" FT /id="PRO_1000069209" 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; 54096 MW; B120824FC2874490 CRC64; MTKSLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYHKYPVDL KLAEEYGVNG IRISIAWSRI FPTGYGEVNP KGVEFYHNLF AECHKRHVEP FVTLHHFDTP EALHSNGDFL NRENIEHFVN YAAFCFEEFP EVRYWTTFNE IGPIGDGQYL VGKFPPGIQY DLAKVFQSHH NMMVSHARAV KLYKDKGYKG EIGVVHALPT KYPYDPENPA DVRAAELEDI IHNKFILDAT YLGHYSDVTL AGVNHILKVN GGQLDLRDED FAALEAAKDL NDFLGINYYM SDWMRDFDGE TEIIHNGKGE KGSSKYQIKG VGRRESPTHI PKTDWDWIIY PQGLYDQIMR IKKDYPNYKK IYITENGLGY KDEFVDNTVY DDARIDYVKQ HLEVLSDAIV DGANVKGYFI WSLMDVFSWS NGYEKRYGLF YVDFETQERY PKKSAHWYKK LAETQMIE //