LACG_STREM
ID LACG_STREM Reviewed; 469 AA.
AC B4U1G6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=Sez_0461;
OS Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=552526;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGCS10565;
RX PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA Musser J.M.;
RT "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT causing epidemic nephritis: new information about an old disease.";
RL PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG61833.1; -; Genomic_DNA.
DR RefSeq; WP_012515109.1; NC_011134.1.
DR AlphaFoldDB; B4U1G6; -.
DR SMR; B4U1G6; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR EnsemblBacteria; ACG61833; ACG61833; Sez_0461.
DR KEGG; sez:Sez_0461; -.
DR HOGENOM; CLU_001859_1_3_9; -.
DR OMA; DWVYVVP; -.
DR UniPathway; UPA00542; UER00605.
DR Proteomes; UP000001873; 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_1000147419"
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; 53462 MW; 26FA2980DE9B644E CRC64;
MIKRLPDDFI FGGATAAYQA EGATTIDGKG AVAWDRYLKD NYWYTAEPAS DFYHQYPIDL
ALAEQFGING IRISIAWSRI FPEGFGEVNA KGVAFYHSLF AECHKHHVEP FVTLHHFDTP
EALHSRGDFL NRENIDHFVA YAAYCFKEFP EVSYWTTFNE IGPIGDGQYL VGKFPPGISY
DLAKVFQSHH NMMLAHARAL VHYKEQAYPG EIGIVHALPT KYPLDPTNPA DVLAAELDDI
IHNKFILDAT YLGQYSEKTM AGVKHILAEN GGSLDLRPED FELLQAAKDL NDFLGINYYM
SDWLRAFDGE TEIIHNGKGE KGGSKYQIKG VGQRIFDVDV PRTDWDWMIY PQGLYDQIMR
IKADYPGYKK IYITENGLGY KDTCIDGRID DDARIDYIKQ HLAVIADVIS AGANVKGYFI
WSLMDVFSWS NGYDKRYGLF YVDFETQKRY PKKSAYWYQQ LAATKTISV
