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Beta-agarase AgaA34

Agarivorans albus
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli


Catalytic activityi

Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.1 Publication


  1. KM=0.117 µM for agarose1 Publication
  2. KM=0.333 µM for neoagarotetraose1 Publication
  1. Vmax=529 µmol/min/mg enzyme toward agarose1 Publication
  2. Vmax=313 µmol/min/mg enzyme toward neoagarotetraose1 Publication

pH dependencei

Optimum pH is 8.0. Active from pH 6.0 to 10.0.1 Publication

Temperature dependencei

Optimum temperature is 40 degrees Celsius. Active at temperatures up to 50 degrees Celsius.1 Publication

GO - Molecular functioni

  • beta-agarase activity Source: UniProtKB

GO - Biological processi

  • carbohydrate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases


Names & Taxonomyi

Protein namesi
Recommended name:
Beta-agarase AgaA341 Publication (EC:
OrganismiAgarivorans albus
Taxonomic identifieri182262 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAgarivorans

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti


PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003473251 – ›10Beta-agarase AgaA34›10

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 16 family.1 Publication


Sequence statusi: Fragment.

Mass (Da):1,053
Last modified:September 2, 2008 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei101 Publication1


3D structure databases


Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases


Family and domain databases


Entry informationi

Entry nameiAGA34_AGAAL
AccessioniPrimary (citable) accession number: P85974
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: October 1, 2014
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program


Keywords - Technical termi

Direct protein sequencing


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

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 one 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.