LACG_STRPJ
ID LACG_STRPJ Reviewed; 468 AA.
AC B8ZQ59;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=SPN23F10850;
OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=561276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700669 / Spain 23F-1;
RX PubMed=19114491; DOI=10.1128/jb.01343-08;
RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA Mitchell T.J.;
RT "Role of conjugative elements in the evolution of the multidrug-resistant
RT pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL J. Bacteriol. 191:1480-1489(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; FM211187; CAR68898.1; -; Genomic_DNA.
DR RefSeq; WP_000169288.1; NC_011900.1.
DR AlphaFoldDB; B8ZQ59; -.
DR SMR; B8ZQ59; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; sne:SPN23F10850; -.
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_1000185575"
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; 53837 MW; 7205F2127CC5F0DC CRC64;
MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYNRYPVDL
KLAEEYGVNG IRISIAWSRI FPTGYGQVNV KGVEFYHNLF AECHKRHVEP FVTLHHFDTP
EALHSNGDFL NRENIEHFVD YAAFCFEEFP EVNYWTTFNE IGPIGDGQYL VGKFPPGIQY
DLAKVFQSHH NMMVSHARAV KLYKEKGYKG EIGVVHALPT KYPLDHENPA DVRAAELEDI
IHNKFILDAT YLGHYSEKTL AGVEAILAAN GGSLDLREED FTALEAAKDL NDFLGINYYM
SDWMEAFDGE TEIIHNGKGE KGSSKYQIKG IGRRVAPDYV PRTDWDWIIY PQGLYDQIMR
VKKDYPNYKK IYITENGLGY KDEFVDNTVY DDGRIDYVKQ HLEVLSDAIA DGANVKGYFI
WSLMDVFSWS NGYEKRYGLF YVDFETQERY PKKSAHWYKK VAETQIID
