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P81669

- BGAL_PINPS

UniProt

P81669 - BGAL_PINPS

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Protein

Putative beta-galactosidase

Gene
N/A
Organism
Pinus pinaster (Maritime pine)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Putative beta-galactosidase (EC:3.2.1.23)
Short name:
Lactase
OrganismiPinus pinaster (Maritime pine)
Taxonomic identifieri71647 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaePinalesPinaceaePinusPinus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›44›44Putative beta-galactosidasePRO_0000057686Add
BLAST

Expressioni

Inductioni

By water stress.

Structurei

3D structure databases

ProteinModelPortaliP81669.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 35 family.Curated

Sequencei

Sequence statusi: Fragments.

P81669-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40 
VNIGVNYGML GNSYPTGPET ERHFGLNPDT LHVVRHAQGF HNLA
Length:44
Mass (Da):4,831
Last modified:July 15, 1999 - v1
Checksum:i30886985FF48C9FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-adjacent residuesi15 – 162Curated
Non-adjacent residuesi29 – 302Curated
Non-terminal residuei44 – 441

Cross-referencesi

3D structure databases

ProteinModelPortali P81669.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Needle.

Entry informationi

Entry nameiBGAL_PINPS
AccessioniPrimary (citable) accession number: P81669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: January 7, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.