ID LACG_CLOAB Reviewed; 474 AA. AC Q97EZ2; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 27-MAR-2024, entry version 114. 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=CA_C2963; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 OS / VKM B-1787). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., RA Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). 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; AE001437; AAK80905.1; -; Genomic_DNA. DR PIR; F97264; F97264. DR RefSeq; NP_349565.1; NC_003030.1. DR RefSeq; WP_010966246.1; NC_003030.1. DR AlphaFoldDB; Q97EZ2; -. DR SMR; Q97EZ2; -. DR STRING; 272562.CA_C2963; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR GeneID; 44999451; -. DR KEGG; cac:CA_C2963; -. DR PATRIC; fig|272562.8.peg.3147; -. DR eggNOG; COG2723; Bacteria. DR HOGENOM; CLU_001859_1_3_9; -. DR OrthoDB; 2339329at2; -. DR UniPathway; UPA00542; UER00605. DR Proteomes; UP000000814; 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; Reference proteome. FT CHAIN 1..474 FT /note="6-phospho-beta-galactosidase" FT /id="PRO_0000260722" FT ACT_SITE 160 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" FT ACT_SITE 374 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" FT BINDING 18 FT /ligand="D-galactose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:91004" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" FT BINDING 115 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 296 FT /ligand="D-galactose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:91004" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" FT BINDING 427 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 434 FT /ligand="D-galactose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:91004" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" FT BINDING 436 FT /ligand="D-galactose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:91004" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574" SQ SEQUENCE 474 AA; 54672 MW; 5661CA39AAC5C3BE CRC64; MNNFGEDFIF GGATAAYQAE GATKEDGKGP CIWDEYLKKE GRFTGDTASD FYHKYKEDLK FSRKFGVNGI RISIAWSRVI PDGKGEVNPK GLKFYSDLID ECIKNNVEPF VTLHHFDTPL TLFKDGDWLN RNNIDYFVRF AKVCFEALGD RVKKWITFNE AWAVAQNGYI IGNFPPSIKY DIPKAAQSMH NMMVAHAKVV ELYKSMNLDG EIGIVHTLEG KYPITDSKED KEAAYLDYMI SNKFMLDACF KGEYPKETEK TINEIMSKNG GELKIYDGDL EVLKKASSKI DFLGMNYYSS HFLKAYEGES RIHHNGTGEK GTSIFALKGI GERVNNPEVP TTDWDWPIYP KGLHDMLVRI KNEYPNYKKI YVTENGMGYK DDFKDGKIDD TPRIDYINKH LEAILKAKNE GVVVKGYFVW SLMDVLSWSN GYNKRYGLFY VDFKTQNRYA KKSAYWFKRI SYEKKLIDFS DIEY //