LACG_LACCB
ID LACG_LACCB Reviewed; 474 AA.
AC B3W7I3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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}; OrderedLocusNames=LCABL_07280;
OS Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=543734;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL23;
RA Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA Deutscher J.;
RT "Lactobacillus casei BL23 complete genome sequence.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FM177140; CAQ65853.1; -; Genomic_DNA.
DR RefSeq; WP_003589794.1; NC_010999.1.
DR AlphaFoldDB; B3W7I3; -.
DR SMR; B3W7I3; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GeneID; 45549901; -.
DR KEGG; lcb:LCABL_07280; -.
DR HOGENOM; CLU_001859_1_3_9; -.
DR OMA; DWVYVVP; -.
DR OrthoDB; 654705at2; -.
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 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 PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR01233; lacG; 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_1000147418"
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"
SQ SEQUENCE 474 AA; 53968 MW; EBE1B0C3A45498C9 CRC64;
MSKQLPQDFV MGGATAAYQV EGATKEDGKG RVLWDDFLDK QGRFKPDPAA DFYHRYDEDL
ALAEKYGHQV IRVSIAWSRI FPDGAGEVEP RGVAFYHKLF ADCAAHHIEP FVTLHHFDTP
ERLHEAGDWL SQEMLDDFVA YAKFCFEEFS EVKYWITINE PTSMAVQQYT SGTFPPAESG
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
