ID   LACG_LEPBD              Reviewed;         467 AA.
AC   C7N8L9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=6-phospho-beta-galactosidase;
DE            EC=3.2.1.85;
DE   AltName: Full=Beta-D-phosphogalactoside galactohydrolase;
DE            Short=PGALase;
DE   AltName: Full=P-beta-Gal;
DE            Short=PBG;
GN   Name=lacG; OrderedLocusNames=Lebu_0590;
OS   Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS   10249 / C-1013-b).
OC   Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Leptotrichia.
OX   NCBI_TaxID=523794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
RX   PubMed=21304648; DOI=10.4056/sigs.1854;
RA   Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA   Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA   Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT   b).";
RL   Stand. Genomic Sci. 1:126-132(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 3-33, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX   PubMed=12351228; DOI=10.1111/j.1574-6968.2002.tb11344.x;
RA   Thompson J.;
RT   "Purification and some properties of phospho-beta-galactosidase from the
RT   Gram-negative oral bacterium Leptotrichia buccalis ATCC 14201.";
RL   FEMS Microbiol. Lett. 214:183-188(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:0000269|PubMed:12351228};
CC   -!- ACTIVITY REGULATION: Inhibited by both galactose-6-phosphate and ATP.
CC       {ECO:0000269|PubMed:12351228}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.54 mM for oNPbetagal6P (at pH 7.5)
CC         {ECO:0000269|PubMed:12351228};
CC         Vmax=50.94 umol/min/mg enzyme with oNPbetagal6P as substrate
CC         {ECO:0000269|PubMed:12351228};
CC       pH dependence:
CC         Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:12351228};
CC   -!- PATHWAY: Carbohydrate metabolism; lactose degradation; D-galactose 6-
CC       phosphate and beta-D-glucose from lactose 6-phosphate: step 1/1.
CC   -!- INDUCTION: Induced during growth on lactose or lactulose.
CC       {ECO:0000269|PubMed:12351228}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; CP001685; ACV38500.1; -; Genomic_DNA.
DR   RefSeq; WP_012806681.1; NC_013192.1.
DR   AlphaFoldDB; C7N8L9; -.
DR   SMR; C7N8L9; -.
DR   STRING; 523794.Lebu_0590; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   EnsemblBacteria; ACV38500; ACV38500; Lebu_0590.
DR   KEGG; lba:Lebu_0590; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_0; -.
DR   OMA; WHVCEHG; -.
DR   OrthoDB; 654705at2; -.
DR   UniPathway; UPA00542; UER00605.
DR   Proteomes; UP000001910; Chromosome.
DR   GO; GO:0033920; F:6-phospho-beta-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0015925; F:galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0005990; P:lactose catabolic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..467
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_0000398183"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  54271 MW;  D8642C3EEC575EC1 CRC64;
     MSKKLPEDFI FGGATAAYQA EGAIKIDGKG PVAWDKFLEE NYWYTAEPAS DFYHQYPVDL
     KLCEEFGING IRISIAWSRI FPNGYGEVNP KGVEFYHKLF AECKKRKVEP FVTLHHFDTP
     EVLHSNGDFL NRENIEHFVN YAKFCFEEFS EVNYWTTFNE IGPIGDGQYL VGKFPPGIKY
     DFEKLFQSHH NMVLAHAKAV NLFKKNGYHG EIGMVCALPT KYPYDPNNPK DVRAAELDDI
     IHNKFILDAT FKGEYSKNTM EGVNHILQVN GGKLDLREED FEELKAAKDL NDFLGINYYM
     SDWMAEYDGE TEIIHNATGN KGSSKYQIKG VGQRKANESI PRTDWDWIIY PQGLYDQISR
     VKKDYPNYKK IYITENGLGY KDVFEDNTVY DDARIDYIRQ HLEVISDAIK DGANVKGYFL
     WSLMDVFSWS NGYEKRYGLF YVDFETQKRY PKKSAYWYKK VSETKEV