ID   LACG_STRA3              Reviewed;         468 AA.
AC   Q8E4S2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 116.
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=gbs1329;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
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; AL766850; CAD46988.1; -; Genomic_DNA.
DR   RefSeq; WP_000169238.1; NC_004368.1.
DR   AlphaFoldDB; Q8E4S2; -.
DR   SMR; Q8E4S2; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; san:gbs1329; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_9; -.
DR   UniPathway; UPA00542; UER00605.
DR   Proteomes; UP000000823; 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.
FT   CHAIN           1..468
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_0000260728"
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         428
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         429
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         435
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   BINDING         437
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
SQ   SEQUENCE   468 AA;  54066 MW;  7AE561F18F85C565 CRC64;
     MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYHKYPVDL
     ALAEEYGVNG IRISIAWSRI FPTGYGEVNL KGVEFYHKLF EECHKRHVEP FVTLHHFDTP
     EALHSNGDFL NRDNIEHFVN YAAFCFEEFP EVNYWTTFNE IGPIGDGQYL VGKFPPGIQY
     DLAKVFQSHH NMMVSHARAV KLYKDKGYKG EIGVVHALPT KYPLDPENSA DVRAAELEDI
     IHNKFILDAT YLGYYSEMTM AGVKHILKEN GGELDLREED FQALEAAKDL NDFLGINYYM
     SDWMQAFDGE TEIIHNGKGE KGSSKYQIKG VGRRVAPDYV PKTDWDWIIY PQGLYDQIMR
     VKNDYPNYKK IYITENGLGY KDEFVDNTVY DDGRIDYVKQ HLEVLSEAIS DGANVKGYFI
     WSLMDVFSWS NGYEKRYGLF YVDFETQERY PKKSAHWYKQ VAKTQIIE
//