LACG_STRPQ
ID LACG_STRPQ Reviewed; 468 AA.
AC P0DB41; Q79W99; Q8K5V1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 54.
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=SPs1651;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
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; BA000034; BAC64746.1; -; Genomic_DNA.
DR RefSeq; WP_011055001.1; NC_004606.1.
DR AlphaFoldDB; P0DB41; -.
DR SMR; P0DB41; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; sps:SPs1651; -.
DR HOGENOM; CLU_001859_1_3_9; -.
DR OMA; DWVYVVP; -.
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..468
FT /note="6-phospho-beta-galactosidase"
FT /id="PRO_0000411358"
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 468 AA; 53874 MW; 511359DDE5476CEE CRC64;
MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYNRYPVDL
KLSEEFGVNG IRISIAWSRI FPTGKGEVNP KGVEYYHNLF AECHKRHVEP FVTLHHFDTP
EALHSDGDFL NRENIEHFVN YAEFCFKEFS EVNYWTTFNE IGPIGDGQYL VGKFPPGIQY
DLAKVFQSHH NMMVSHARAV KLFKDSGYSG EIGVVHALPT KYPFDANNPD DVRAAELEDI
IHNKFILDAT YLGKYSDKTM EGVNHILEVN GGELDLREED FAALDAAKDL NDFLGINYYM
SDWMQAFDGE TEIIHNGKGE KGSSKYQIKG VGRRKAPVDV PKTDWDWIIF PQGLYDQIMR
VKADYPNYKK IYITENGLGY KDEFVDNTVY DDGRIDYVKK HLEVISDAIS DGVNVKGYFM
WSLMDVFSWS NGYEKRYGLF YVDFETQERY PKKSAYWYKK VAETQVIE