LACG_STRMU
ID LACG_STRMU Reviewed; 468 AA.
AC P50978;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 138.
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=SMU_1490;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700611 / UA130 / Serotype c;
RX PubMed=8277252; DOI=10.1099/00221287-139-11-2685;
RA Honeyman A.L., Curtiss R. III;
RT "Isolation, characterization and nucleotide sequence of the Streptococcus
RT mutans lactose-specific enzyme II (lacE) gene of the PTS and the phospho-
RT beta-galactosidase (lacG) gene.";
RL J. Gen. Microbiol. 139:2685-2694(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; L18993; AAA16450.1; -; Unassigned_DNA.
DR EMBL; AE014133; AAN59144.1; -; Genomic_DNA.
DR RefSeq; NP_721838.1; NC_004350.2.
DR RefSeq; WP_002263058.1; NC_004350.2.
DR AlphaFoldDB; P50978; -.
DR SMR; P50978; -.
DR STRING; 210007.SMU_1490; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR EnsemblBacteria; AAN59144; AAN59144; SMU_1490.
DR KEGG; smu:SMU_1490; -.
DR PATRIC; fig|210007.7.peg.1326; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_3_9; -.
DR OMA; DWVYVVP; -.
DR PhylomeDB; P50978; -.
DR SABIO-RK; P50978; -.
DR UniPathway; UPA00542; UER00605.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0033920; F:6-phospho-beta-galactosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:CACAO.
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; Reference proteome.
FT CHAIN 1..468
FT /note="6-phospho-beta-galactosidase"
FT /id="PRO_0000063893"
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"
FT CONFLICT 150
FT /note="P -> S (in Ref. 1; AAA16450)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="M -> I (in Ref. 1; AAA16450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 53762 MW; FEDBDCE1E23D84F7 CRC64;
MSKTLPKDFI FGGATAAYQA EGATHADGKG PVAWDKYLED NYWYTAEPAS DFYHQYPVDL
KLAEEFGVNG IRISIAWSRI FPKGYGAVNP KGLAFYHNLF AECHKRHVEP FVTLHHFDTP
EALHSNGDFL NRENIEHFVN YAEFCFKEFP EVNYWTTFNE IGPIGDGQYL VGKFPPGIQY
DLAKVFQSHH NMMVAHSKAV KLFKDGGYSG EIGVVHALPT KYPYDPNNPA DIRAAELEDI
IHNKFILDAT YLGKYSEKTM EGVNHILAVN GGQLDLREED FAALEAAKDL NDFLGINYYM
SDWMRAFDGE TEITHNAKGE KGSSKYQIKG VGRREAPVNV PKTDWDWIIY PQGLYDQIMR
VKQDYPNYKK IYITENGLGY KDEFVNHTVY DDARIDYVKK HLEVLSDAIA DGANVKGYFI
WSLMDVFSWS NGYEKRYGLF YVDFDTQERY PKKSAYWYKK LAETQIID
