LACG_LACLL
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 25-MAY-2022, entry version 126.
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, ECO:0000303|PubMed:2515252};
OS Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG Plasmid pUCL13, and Plasmid pLP712.
OC Bacteria; Firmicutes; 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]
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]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
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 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 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 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
