ID   LACG_LACRH              Reviewed;         474 AA.
AC   Q29ZJ1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
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 rhamnosus (Lactobacillus rhamnosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=47715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TCELL-1;
RX   PubMed=16478484; DOI=10.1111/j.1365-2672.2005.02790.x;
RA   Tsai Y.-K., Lin T.-H.;
RT   "Sequence, organization, transcription and regulation of lactose and
RT   galactose operons in Lactobacillus rhamnosus TCELL-1.";
RL   J. Appl. Microbiol. 100:446-459(2006).
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; AY705915; AAW30155.1; -; Genomic_DNA.
DR   RefSeq; WP_005691814.1; NZ_WPCQ01000010.1.
DR   AlphaFoldDB; Q29ZJ1; -.
DR   SMR; Q29ZJ1; -.
DR   STRING; 568703.LGG_00650; -.
DR   eggNOG; COG2723; Bacteria.
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; 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.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..474
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_0000260723"
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;  53727 MW;  E115E26364815405 CRC64;
     MRKQLPKDFV IGGATAAYQV EGATKEDGKG RVLWDDFLEK QGRFSPDPAA DFYHRYDEDL
     ALAEAYGHQV IRLSIAWSRI FPDGAGAVEP RGVAFYHRLF AACAKHHLIP FVTLHHFDTP
     ERLHAIGDWL SQEMLEDFVE YARFCFEEFP EIKHWITINE PTSMAVQQYT SGTFPPAETG
     HFDKTFQAEH NQIVAHARIV NLYKSMGLDG EIGIVHALQT PYPYSDSSED QHAADLQDAL
     ENRLYLDGTL AGDYAPKTLA LIKEILAANQ QPMFKYTDEE MAAIKKAAHQ LDFVGVNNYF
     SKWLRAYHGK SETIHNGDGS KGSSVARLHG IGEEKKPAGI ETTDWDWSIY PRGMYDMLMR
     IHQDYPLVPA IYVTENGIGL KESLPAEVTP NTVIADPKRI DYLKKYLSAV ADAIQAGANV
     KGYFVWSLQD QFSWTNGYSK RYGLFFVDFP TQKRYVKQSA EWLKQVSQTH VIPE