LACG_STAAB
ID LACG_STAAB Reviewed; 470 AA.
AC Q2YYJ9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=SAB2070c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81759.1; -; Genomic_DNA.
DR RefSeq; WP_000169224.1; NC_007622.1.
DR AlphaFoldDB; Q2YYJ9; -.
DR SMR; Q2YYJ9; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; sab:SAB2070c; -.
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..470
FT /note="6-phospho-beta-galactosidase"
FT /id="PRO_0000260724"
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 470 AA; 54565 MW; 9A5C8E295AB8DF2F CRC64;
MTKTLPEDFI FGGATAAYQA EGATNTDGKG RVAWDTYLEE NYWYTAEPAS DFYNRYPVDL
ELSEKFGVNG IRISIAWSRI FPNGYGEVNP KGVEYYHKLF AECHKRHVEP FVTLHHFDTP
EVLHKDGDFL NRKTIDYFVD YAEYCFKEFP EVKYWTTFNE IGPIGDGQYL VGKFPPGIKY
DFEKVFQSHH NMMVAHARAV KLFKDGGYQG EIGVVHALPT KYPFDPSNPE DVRAAELEDI
IHNKFILDAT YLGKYSRETM EGVQHILSVN GGKLNITDED YAILDAAKDL NDFLGINYYM
SDWMRGYDGE SEITHNATGD KGGSKYQLKG VGQREFDVDV PRTDWDWMIY PQGLYDQIMR
VVKDYPNYHK IYITENGLGY KDEFIESEKT VHDDARIDYV RQHLNVIADA IKDGANVKGY
FIWSLMDVFS WSNGYEKRYG LFYVDFETQE RYPKKSAYWY KELAETKEIK
