LACG_STAHJ
ID LACG_STAHJ Reviewed; 469 AA.
AC Q4L868;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=SH0848;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04157.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4L868; -.
DR SMR; Q4L868; -.
DR STRING; 279808.SH0848; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR EnsemblBacteria; BAE04157; BAE04157; SH0848.
DR KEGG; sha:SH0848; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_3_9; -.
DR OMA; DWVYVVP; -.
DR OrthoDB; 654705at2; -.
DR UniPathway; UPA00542; UER00605.
DR Proteomes; UP000000543; 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_0000260727"
FT ACT_SITE 159
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT ACT_SITE 374
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
SQ SEQUENCE 469 AA; 54646 MW; 0D933E94BF925793 CRC64;
MKKLPEDFIF GGATAAYQAE GATQTDGKGR VAWDTYLEEN YWYTAEPASD FYNKYPIDLE
LSEKFGVNGI RISIAWSRIF PKGYGEVNPK GVEYYHNLFK ECHRRHVEPF VTLHHFDTPE
TLHSDGDFLN RKTIEYFVEY AKFCFEEFEE VNYWTTFNEI GPIGDGQYLV GKFPPGIKYD
FAKVFQSHHN MMVAHAKAVK LFKDNGYSGE VGVVHALPTK YPYDPTNPED VRAAELEDII
HNKFILDATY LGKYSRETME GVQHILSVNG GKLDIPEEDY KVLEAAKDLN DFLGINYYMS
DWMRGYDGES EITHNATGDK GGSKYQLKGV GQREFDVDVP RTDWDWMIYP KGLYDQIMRV
VKDYPNYHKI YITENGLGYK DQFDEERKTV DDDARIDYVK KHLEVISDAI RDGANVKGYF
IWSLMDVFSW SNGYEKRYGL FYVDFETQER YPKKSAYWYK ELAESKEIK