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Reviewed, UniProtKB/Swiss-Prot P81669 (BGAL_PINPS)

Last modified November 24, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative beta-galactosidase
      Short name=Lactase
    EC=3.2.1.23
OrganismPinus pinaster (Maritime pine)
Taxonomic identifier71647 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaConiferopsidaConiferalesPinaceaePinusPinus

Protein attributes

Sequence length44 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Induction

By water stress.

Miscellaneous

On the 2D-gel the determined pI of this protein (spot N76) is: 5.8, its MW is: 32 kDa.

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Ontologies

Keywords
   Biological processStress response
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbeta-galactosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›44›44Putative beta-galactosidase
PRO_0000057686

Experimental info

Non-adjacent residues15 – 162
Non-adjacent residues29 – 302
Non-terminal residue11
Non-terminal residue441

Sequences

Sequence LengthMass (Da)Tools
P81669-1 [UniParc].

Last modified July 15, 1999. Version 1.
Checksum: 30886985FF48C9FA

FASTA444,831
        10         20         30         40 
VNIGVNYGML GNSYPTGPET ERHFGLNPDT LHVVRHAQGF HNLA 

« Hide

References

[1]"Separation and characterization of needle and xylem maritime pine proteins."
Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A., Frigerio J.-M., Plomion C.
Electrophoresis 20:1098-1108(1999) [PubMed: 10344291] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Needle.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.23. 97638.

Family and domain databases

PROSITEPS01182. GLYCOSYL_HYDROL_F35. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGAL_PINPS
AccessionPrimary (citable) accession number: P81669
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 24, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents