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P50978 (LACG_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:SMU_1490
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlactose catabolic process via tagatose-6-phosphate

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phospho-beta-galactosidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4684686-phospho-beta-galactosidase HAMAP-Rule MF_01574
PRO_0000063893

Sites

Active site1601Proton donor By similarity
Active site3751Nucleophile By similarity

Experimental info

Sequence conflict1501P → S in AAA16450. Ref.1
Sequence conflict3001M → I in AAA16450. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50978 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: FEDBDCE1E23D84F7

FASTA46853,762
        10         20         30         40         50         60 
MSKTLPKDFI FGGATAAYQA EGATHADGKG PVAWDKYLED NYWYTAEPAS DFYHQYPVDL 

        70         80         90        100        110        120 
KLAEEFGVNG IRISIAWSRI FPKGYGAVNP KGLAFYHNLF AECHKRHVEP FVTLHHFDTP 

       130        140        150        160        170        180 
EALHSNGDFL NRENIEHFVN YAEFCFKEFP EVNYWTTFNE IGPIGDGQYL VGKFPPGIQY 

       190        200        210        220        230        240 
DLAKVFQSHH NMMVAHSKAV KLFKDGGYSG EIGVVHALPT KYPYDPNNPA DIRAAELEDI 

       250        260        270        280        290        300 
IHNKFILDAT YLGKYSEKTM EGVNHILAVN GGQLDLREED FAALEAAKDL NDFLGINYYM 

       310        320        330        340        350        360 
SDWMRAFDGE TEITHNAKGE KGSSKYQIKG VGRREAPVNV PKTDWDWIIY PQGLYDQIMR 

       370        380        390        400        410        420 
VKQDYPNYKK IYITENGLGY KDEFVNHTVY DDARIDYVKK HLEVLSDAIA DGANVKGYFI 

       430        440        450        460 
WSLMDVFSWS NGYEKRYGLF YVDFDTQERY PKKSAYWYKK LAETQIID 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, characterization and nucleotide sequence of the Streptococcus mutans lactose-specific enzyme II (lacE) gene of the PTS and the phospho-beta-galactosidase (lacG) gene."
Honeyman A.L., Curtiss R. III
J. Gen. Microbiol. 139:2685-2694(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 700611 / UA130 / Serotype c.
[2]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18993 Unassigned DNA. Translation: AAA16450.1.
AE014133 Genomic DNA. Translation: AAN59144.1.
RefSeqNP_721838.1. NC_004350.2.

3D structure databases

ProteinModelPortalP50978.
SMRP50978. Positions 1-468.
ModBaseSearch...

Protein-protein interaction databases

STRING210007.SMU.1490.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN59144; AAN59144; SMU_1490.
GeneID1028734.
KEGGsmu:SMU_1490.
PATRIC19664995. VBIStrMut61772_1326.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2723.
KOK01220.
OMAFKDGGYS.
ProtClustDBPRK13511.

Enzyme and pathway databases

SABIO-RKP50978.
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. Glyco_hydro_cat. 1 hit.
TIGRFAMsTIGR01233. lacG. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLACG_STRMU
AccessionPrimary (citable) accession number: P50978
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 28, 2002
Last modified: May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families