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P11546 (LACG_LACLL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phospho-beta-galactosidase

EC=3.2.1.85
Alternative name(s):
Beta-D-phosphogalactoside galactohydrolase
Short name=PGALase
P-beta-Gal
Short name=PBG
Gene names
Name:lacG
Encoded onPlasmid pUCL13 Ref.1
Plasmid pLP712 Ref.2
OrganismLactococcus lactis subsp. lactis (Streptococcus lactis)
Taxonomic identifier1360 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

A 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol. HAMAP-Rule MF_01574

Pathway

Carbohydrate metabolism; lactose degradation; D-galactose 6-phosphate and beta-D-glucose from lactose 6-phosphate: step 1/1. HAMAP-Rule MF_01574

Induction

By lactose. The operon consists of lacABCDFEGX. Ref.3

Miscellaneous

This gene was sequenced from pMG820, a laboratory-derived deletion of the naturally occurring plasmid pLP712.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Sequence caution

The sequence AAA26949.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA42986.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4684686-phospho-beta-galactosidase HAMAP-Rule MF_01574
PRO_0000063883

Sites

Active site1601Proton donor
Active site3751Nucleophile

Experimental info

Sequence conflict3831E → Q in AAA25173. Ref.1
Sequence conflict3871N → K in AAA25173. Ref.1

Secondary structure

..................................................................................... 468
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11546 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 5ACFC9BB81DF0E90

FASTA46854,072
        10         20         30         40         50         60 
MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYHKYPVDL 

        70         80         90        100        110        120 
ELAEEYGVNG IRISIAWSRI FPTGYGEVNE KGVEFYHKLF AECHKRHVEP FVTLHHFDTP 

       130        140        150        160        170        180 
EALHSNGDFL NRENIEHFID YAAFCFEEFP EVNYWTTFNE IGPIGDGQYL VGKFPPGIKY 

       190        200        210        220        230        240 
DLAKVFQSHH NMMVSHARAV KLYKDKGYKG EIGVVHALPT KYPYDPENPA DVRAAELEDI 

       250        260        270        280        290        300 
IHNKFILDAT YLGHYSDKTM EGVNHILAEN GGELDLRDED FQALDAAKDL NDFLGINYYM 

       310        320        330        340        350        360 
SDWMQAFDGE TEIIHNGKGE KGSSKYQIKG VGRRVAPDYV PRTDWDWIIY PEGLYDQIMR 

       370        380        390        400        410        420 
VKNDYPNYKK IYITENGLGY KDEFVDNTVY DDGRIDYVKQ HLEVLSDAIA DGANVKGYFI 

       430        440        450        460 
WSLMDVFSWS NGYEKRYGLF YVDFDTQERY PKKSAHWYKK LAETQVIE 

« Hide

References

[1]"Isolation and structural analysis of the phospho-beta-galactosidase gene from Streptococcus lactis Z268."
Boizet B., Villeval D., Slos P., Novel M., Novel G., Mercenier A.
Gene 62:249-261(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: L13 / Z268.
[2]"Structure and expression of the Lactococcus lactis gene for phospho-beta-galactosidase (lacG) in Escherichia coli and L. lactis."
de Vos W.M., Gasson M.J.
J. Gen. Microbiol. 135:1833-1846(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
Strain: 712.
[3]"Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis."
de Vos W.M., Boerrigter I.J., van Rooyen R.J., Reiche B., Hengstenberg W.
J. Biol. Chem. 265:22554-22560(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE, INDUCTION.
Strain: MG1820.
[4]"Nonidentity between plasmid and chromosomal copies of ISS1-like sequences in Lactococcus lactis subsp. lactis CNRZ270 and their possible role in chromosomal integration of plasmid genes."
Huang D.C., Novel M., Huang X.F., Novel G.
Gene 118:39-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-468.
Strain: Z270.
[5]"The three-dimensional structure of 6-phospho-beta-galactosidase from Lactococcus lactis."
Wiesmann C., Beste G., Hengstenberg W., Schulz G.E.
Structure 3:961-968(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[6]"Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis."
Wiesmann C., Hengstenberg W., Schulz G.E.
J. Mol. Biol. 269:851-860(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28357 Genomic DNA. Translation: AAA25173.1.
M60447 Genomic DNA. Translation: AAA25183.1.
M19454 Genomic DNA. Translation: AAA26949.1. Different initiation.
X60456 Genomic DNA. Translation: CAA42986.1. Different initiation.
PIRGLSOPL. A37168.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PBGX-ray2.30A/B1-468[»]
2PBGX-ray2.50A1-468[»]
3PBGX-ray2.70A/B1-468[»]
4PBGX-ray2.50A/B1-468[»]
ProteinModelPortalP11546.
SMRP11546. Positions 1-468.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP11546.
UniPathwayUPA00542; UER00605.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
HAMAPMF_01574. LacG.
InterProIPR005928. 6P-beta-galactosidase.
IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR01233. lacG. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11546.

Entry information

Entry nameLACG_LACLL
AccessionPrimary (citable) accession number: P11546
Secondary accession number(s): Q79AQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries