ID   LACG_STRS7              Reviewed;         469 AA.
AC   C0MDS5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=SZO_15220;
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204884; CAX00199.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MDS5; -.
DR   SMR; C0MDS5; -.
DR   EnsemblBacteria; CAX00199; CAX00199; SZO_15220.
DR   KEGG; seq:SZO_15220; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_9; -.
DR   OMA; DWVYVVP; -.
DR   UniPathway; UPA00542; UER00605.
DR   Proteomes; UP000001368; 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   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..469
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_1000215584"
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   469 AA;  53509 MW;  849F2FFA4A9F4813 CRC64;
     MIKRLPDDFI FGGATAAYQA EGATTIDGKG AVAWDRYLKD NYWYTAEPAS DFYHQYPVDL
     ALAEQFGING IRISIAWSRI FPEGFGEVNA KGVAFYHSLF AECHKHHVEP FVTLHHFDTP
     EALHSRGDFL NRENIDHFVA YAAYCFKEFP EVTYWTTFNE IGPIGDGQYL VGKFPPGISY
     DLAKVFQSHH NMMLAHARAL VHYKEQAYPG EIGIVHALPT KYPLDPKKPG DVLAAELDDI
     IHNKFILDAT YLGQYSEKTM AGVKHILAEN GGSLDLRPED FELLQAAKDL NDFLGINYYM
     SDWLRAFDGE TEIIHNGKGE KGGSKYQIKG VGQRVFDVDV PRTDWDWMIY PQGLYDQIMR
     IKADYPGYKK IYITENGLGY KDTCIDGRID DDARIDYIKQ HLAVIADAIS TGANVKGYFI
     WSLMDVFSWS NGYDKRYGLF YVDFETQKRY PKKSAYWYQQ LAATKTISM