LACG_STRU0
ID LACG_STRU0 Reviewed; 468 AA.
AC B9DU98;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=SUB0800;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(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; AM946015; CAR41805.1; -; Genomic_DNA.
DR RefSeq; WP_012658310.1; NC_012004.1.
DR AlphaFoldDB; B9DU98; -.
DR SMR; B9DU98; -.
DR STRING; 218495.SUB0800; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR EnsemblBacteria; CAR41805; CAR41805; SUB0800.
DR KEGG; sub:SUB0800; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_3_9; -.
DR OMA; DWVYVVP; -.
DR OrthoDB; 654705at2; -.
DR UniPathway; UPA00542; UER00605.
DR Proteomes; UP000000449; 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; Reference proteome.
FT CHAIN 1..468
FT /note="6-phospho-beta-galactosidase"
FT /id="PRO_1000185576"
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; 53815 MW; 91C61BEC009BAE98 CRC64;
MTKTLPKDFI FGGATAAYQA EGATKTDGKG PVAWDKYLED NYWYTAEPAS DFYNRYPVDL
KLAEEYNVNG IRISIAWSRV FPTGYGEVNR KGVEYYHNLF AECHKRGVEP FVTLHHFDTP
EALHSNGDFL NRDNIDHFVA YAAFCFEEFP EVNYWTTFNE IGPIGDGQYL VGKFPPGIQY
DLAKVFQSHH NMMVSHARAV KLYKDKGYKG EIGVVHALPT KYPYDPANPD DVRAAELEDI
IHNKFILDAT YLGRYSEKTM EGVQHILAAN GGELDLREED FSILEAAKDL NDFLGINYYM
SDWMQAFDGE TEIIHNGKGE KGSSKYQIKG VGRREAPVNV PKTDWDWIIY PQGLYDQIMR
VKADYPNYKK IYITENGLGY KDEFVDGTVY DDGRIDYVKK HLEVISDAIS DGANVKGYFI
WSLMDVFSWS NGYEKRYGLF YVDFETQERY PKKSAHWYKK VAETQVID