ID LACG_LACCA Reviewed; 474 AA. AC P14696; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, 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}; OS Lacticaseibacillus casei (Lactobacillus casei). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lacticaseibacillus. OX NCBI_TaxID=1582; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3130295; DOI=10.1016/0378-1119(88)90564-1; RA Porter E.V., Chassy B.M.; RT "Nucleotide sequence of the beta-D-phosphogalactoside galactohydrolase gene RT of Lactobacillus casei: comparison to analogous pbg genes of other Gram- RT positive organisms."; RL Gene 62:263-276(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 393 / DSM 20011 / JCM 1134 / BCRC 10697 / CCUG 21451 / RC NBRC 15883 / NCIMB 11970 / NCDO 161 / WDCM 00100; RX PubMed=9066115; DOI=10.1111/j.1574-6968.1997.tb10271.x; RA Gosalbes M.J., Monedero V., Alpert C.-A., Perez-Martinez G.; RT "Establishing a model to study the regulation of the lactose operon in RT Lactobacillus casei."; RL FEMS Microbiol. Lett. 148:83-89(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 384-474. RX PubMed=3130296; DOI=10.1016/0378-1119(88)90565-3; RA Alpert C.-A., Chassy B.M.; RT "Molecular cloning and nucleotide sequence of the factor IIIlac gene of RT Lactobacillus casei."; RL Gene 62:277-288(1988). 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; M20151; AAD15134.1; -; Genomic_DNA. DR EMBL; Z80834; CAB02557.1; -; Genomic_DNA. DR EMBL; M20150; AAA25238.1; ALT_SEQ; Genomic_DNA. DR PIR; A29897; A29897. DR PIR; A29898; A29898. DR AlphaFoldDB; P14696; -. DR SMR; P14696; -. DR STRING; 1582.AAW28_06695; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR eggNOG; COG2723; Bacteria. DR SABIO-RK; P14696; -. 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..474 FT /note="6-phospho-beta-galactosidase" FT /id="PRO_0000063882" 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 433 FT /ligand="D-galactose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:91004" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" FT BINDING 434 FT /ligand="D-galactose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:91004" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" FT BINDING 440 FT /ligand="D-galactose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:91004" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" FT BINDING 442 FT /ligand="D-galactose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:91004" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" SQ SEQUENCE 474 AA; 53982 MW; 1FF1B185E3549A9F CRC64; MSKQLPQDFV MGGATAAYQV EGATKEDGKG RVLWDDFLDK QGRFKPDPAA DFYHRYDEDL ALAEKYGHQV IRVSIAWSRI FPDGAGEVEP RGVAFYHKLF ADCAAHHIEP FVTLHHFDTP ERLHEAGDWL SQEMLDDFVA YAKFCFEEFS EVKYWITINE PTSMAVQQYT TGTFPPAESG RFDKTFQAEH NQMVAHARIV NLYKSMQLGG QIGIVHALQT VYPYSDSAVD HHAAELQDAL ENRLYLDGTL AGEYHQETLA LVKEILDANH QPMFQSTPQE MKAIDEAAHQ LDFVGVNNYF SKWLRAYHGK SETIHNGDGT KGSSVARLQG VGEEKLPDGI ETTDWDWSIY PRGMYDILMR IHNDYPLVPV TYVTENGIGL KESLPENATP DTVIEDPKRI DYVKKYLSAM ADAIHDGANV KGYFIWSLQD QFSWTNGYSK RYGLFFVDFP TQNRYIKQSA EWFKSVSETH IIPD //