ID   LACG_LACLL              Reviewed;         468 AA.
AC   P11546; Q79AQ5;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=6-phospho-beta-galactosidase {ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000303|PubMed:8535789};
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, ECO:0000303|PubMed:3130294};
DE            Short=PGALase {ECO:0000255|HAMAP-Rule:MF_01574};
DE   AltName: Full=P-beta-Gal {ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000303|PubMed:3130294};
DE            Short=PBG {ECO:0000255|HAMAP-Rule:MF_01574};
GN   Name=lacG {ECO:0000255|HAMAP-Rule:MF_01574,
GN   ECO:0000303|PubMed:2515252};
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG   Plasmid pUCL13, and Plasmid pLP712.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L13 / Z268; PLASMID=pUCL13;
RX   PubMed=3130294; DOI=10.1016/0378-1119(88)90563-x;
RA   Boizet B., Villeval D., Slos P., Novel M., Novel G., Mercenier A.;
RT   "Isolation and structural analysis of the phospho-beta-galactosidase gene
RT   from Streptococcus lactis Z268.";
RL   Gene 62:249-261(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC   STRAIN=712; PLASMID=pLP712;
RX   PubMed=2515252; DOI=10.1099/00221287-135-7-1833;
RA   de Vos W.M., Gasson M.J.;
RT   "Structure and expression of the Lactococcus lactis gene for phospho-beta-
RT   galactosidase (lacG) in Escherichia coli and L. lactis.";
RL   J. Gen. Microbiol. 135:1833-1846(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE, AND INDUCTION.
RC   STRAIN=MG1820;
RX   PubMed=2125052; DOI=10.1016/s0021-9258(18)45741-9;
RA   de Vos W.M., Boerrigter I.J., van Rooyen R.J., Reiche B., Hengstenberg W.;
RT   "Characterization of the lactose-specific enzymes of the phosphotransferase
RT   system in Lactococcus lactis.";
RL   J. Biol. Chem. 265:22554-22560(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-468.
RC   STRAIN=Z270;
RX   PubMed=1339371; DOI=10.1016/0378-1119(92)90246-l;
RA   Huang D.C., Novel M., Huang X.F., Novel G.;
RT   "Nonidentity between plasmid and chromosomal copies of ISS1-like sequences
RT   in Lactococcus lactis subsp. lactis CNRZ270 and their possible role in
RT   chromosomal integration of plasmid genes.";
RL   Gene 118:39-46(1992).
RN   [5] {ECO:0007744|PDB:1PBG}
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND ACTIVE SITES.
RX   PubMed=8535789; DOI=10.1016/s0969-2126(01)00230-1;
RA   Wiesmann C., Beste G., Hengstenberg W., Schulz G.E.;
RT   "The three-dimensional structure of 6-phospho-beta-galactosidase from
RT   Lactococcus lactis.";
RL   Structure 3:961-968(1995).
RN   [6] {ECO:0007744|PDB:2PBG, ECO:0007744|PDB:3PBG, ECO:0007744|PDB:4PBG}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH BETA-D-GALACTOSE
RP   6-PHOSPHATE.
RX   PubMed=9223646; DOI=10.1006/jmbi.1997.1084;
RA   Wiesmann C., Hengstenberg W., Schulz G.E.;
RT   "Crystal structures and mechanism of 6-phospho-beta-galactosidase from
RT   Lactococcus lactis.";
RL   J. Mol. Biol. 269:851-860(1997).
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   -!- INDUCTION: By lactose. The operon consists of lacABCDFEGX.
CC       {ECO:0000269|PubMed:2125052}.
CC   -!- MISCELLANEOUS: This gene was sequenced from pMG820, a laboratory-
CC       derived deletion of the naturally occurring plasmid pLP712.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01574}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA42986.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M28357; AAA25173.1; -; Genomic_DNA.
DR   EMBL; M60447; AAA25183.1; -; Genomic_DNA.
DR   EMBL; M19454; AAA26949.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X60456; CAA42986.1; ALT_INIT; Genomic_DNA.
DR   PIR; A37168; GLSOPL.
DR   PDB; 1PBG; X-ray; 2.30 A; A/B=1-468.
DR   PDB; 2PBG; X-ray; 2.50 A; A=1-468.
DR   PDB; 3PBG; X-ray; 2.70 A; A/B=1-468.
DR   PDB; 4PBG; X-ray; 2.50 A; A/B=1-468.
DR   PDBsum; 1PBG; -.
DR   PDBsum; 2PBG; -.
DR   PDBsum; 3PBG; -.
DR   PDBsum; 4PBG; -.
DR   AlphaFoldDB; P11546; -.
DR   SMR; P11546; -.
DR   DrugBank; DB02312; beta-D-galactose 6-phosphate.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   BRENDA; 3.2.1.85; 2903.
DR   SABIO-RK; P11546; -.
DR   UniPathway; UPA00542; UER00605.
DR   EvolutionaryTrace; P11546; -.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
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   NCBIfam; TIGR01233; lacG; 1.
DR   PANTHER; PTHR10353:SF340; 6-PHOSPHO-BETA-GALACTOSIDASE 1; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Plasmid.
FT   CHAIN           1..468
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_0000063883"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000305|PubMed:8535789"
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000305|PubMed:8535789"
FT   BINDING         19
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   BINDING         116
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   BINDING         159
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   BINDING         160
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   BINDING         297
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   BINDING         428
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   BINDING         429
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   BINDING         435
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   BINDING         437
FT                   /ligand="D-galactose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:91004"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574,
FT                   ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG"
FT   CONFLICT        383
FT                   /note="E -> Q (in Ref. 1; AAA25173)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="N -> K (in Ref. 1; AAA25173)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           17..20
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:2PBG"
FT   HELIX           34..39
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:2PBG"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           52..65
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           90..106
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          109..117
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           121..125
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           133..148
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          154..159
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           161..169
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:2PBG"
FT   HELIX           182..205
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          209..217
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          221..225
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           229..242
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           244..251
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           257..270
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           278..287
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   TURN            288..290
FT                   /evidence="ECO:0007829|PDB:4PBG"
FT   STRAND          293..297
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          302..305
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:2PBG"
FT   STRAND          325..328
FT                   /evidence="ECO:0007829|PDB:2PBG"
FT   TURN            329..331
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          332..334
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          338..340
FT                   /evidence="ECO:0007829|PDB:2PBG"
FT   HELIX           352..364
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           366..368
FT                   /evidence="ECO:0007829|PDB:2PBG"
FT   STRAND          371..375
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           392..410
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          415..421
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   TURN            429..431
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           432..434
FT                   /evidence="ECO:0007829|PDB:2PBG"
FT   STRAND          439..442
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   TURN            444..446
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   STRAND          449..451
FT                   /evidence="ECO:0007829|PDB:1PBG"
FT   HELIX           453..464
FT                   /evidence="ECO:0007829|PDB:1PBG"
SQ   SEQUENCE   468 AA;  54072 MW;  5ACFC9BB81DF0E90 CRC64;
     MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYHKYPVDL
     ELAEEYGVNG IRISIAWSRI FPTGYGEVNE KGVEFYHKLF AECHKRHVEP FVTLHHFDTP
     EALHSNGDFL NRENIEHFID YAAFCFEEFP EVNYWTTFNE IGPIGDGQYL VGKFPPGIKY
     DLAKVFQSHH NMMVSHARAV KLYKDKGYKG EIGVVHALPT KYPYDPENPA DVRAAELEDI
     IHNKFILDAT YLGHYSDKTM EGVNHILAEN GGELDLRDED FQALDAAKDL NDFLGINYYM
     SDWMQAFDGE TEIIHNGKGE KGSSKYQIKG VGRRVAPDYV PRTDWDWIIY PEGLYDQIMR
     VKNDYPNYKK IYITENGLGY KDEFVDNTVY DDGRIDYVKQ HLEVLSDAIA DGANVKGYFI
     WSLMDVFSWS NGYEKRYGLF YVDFDTQERY PKKSAHWYKK LAETQVIE
//