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LACG_STAA1
ID   LACG_STAA1              Reviewed;         470 AA.
AC   A7X569;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=SAHV_2173;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(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; AP009324; BAF79056.1; -; Genomic_DNA.
DR   RefSeq; WP_000169224.1; NC_009782.1.
DR   AlphaFoldDB; A7X569; -.
DR   SMR; A7X569; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; saw:SAHV_2173; -.
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_1000069207"
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
 
 
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