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Unreviewed, UniProtKB/TrEMBL Q9RGX9 (Q9RGX9_9FLAO)

Last modified June 16, 2009. Version 38. Feed History...

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

Names and origin

Protein namesSubmitted name:
    Beta-agarase A EMBL AAF21820.1
    EC=3.2.1.81
Gene names
Name: agaA EMBL AAF21820.1
OrganismZobellia galactanivorans EMBL AAF21820.1
Taxonomic identifier63186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriaFlavobacterialesFlavobacteriaceaeZobellia

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionbeta-agarase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential EMBL AAF21820.1
Chain20 – 539520 Potential EMBL AAF21820.1
PRO_5000055268
Chain20 – 295276beta-agarase A EMBL AAF21820.1
PRO_5000055269

Sequences

Sequence LengthMass (Da)Tools
Q9RGX9-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 611AA1B1C509563A

FASTA53959,994
        10         20         30         40         50         60 
MKKNYLLLYF IFLLCGSIAA QDWNGIPVPA NPGNGMTWQL QDNVSDSFNY TSSEGNRPTA 

        70         80         90        100        110        120 
FTSKWKPSYI NGWTGPGSTI FNAAQAWTNG SQLAIQAQPA GNGKSYNGII TSKNKIQYPV 

       130        140        150        160        170        180 
YMEIKAKIMD QVLANAFWTL TDDETQEIDI MEGYGSDRGG TWFAQRMHLS HHTFIRNPFT 

       190        200        210        220        230        240 
DYQPMGDATW YYNGGTPWRS AYHRYGCYWK DPFTLEYYID GVKVRTVTRA EIDPNNHLGG 

       250        260        270        280        290        300 
TGLNQATNII IDCENQTDWR PAATQEELAD DSKNIFWVDW IRVYKPVAVS GGGNNGNDGA 

       310        320        330        340        350        360 
TEFQYDLGTD TSAVWPGYTR VSNTTRAGNF GWANTNDIGS RDRGASNGRN NINRDINFSS 

       370        380        390        400        410        420 
QTRFFTQDLS NGTYNVLITF GDTYARKNMN VAAEGQNKLT NINTNAGQYV SRSFDVNVND 

       430        440        450        460        470        480 
GKLDLRFSVG NGGDVWSITR IWIRKVTSNS ANLLAAKGLT LEDPVETTEF LYPNPAKTDD 

       490        500        510        520        530 
FVTVPNSEIG SSIIIYNSAG QVVKKVSVVS ENQKISLEGF AKGMYFINLN GQSTKLIVQ 

« Hide

References

[1]"The endo-beta-agarases AgaA and AgaB from the marine bacterium Zobellia galactanivorans: two paralogue enzymes with different molecular organizations and catalytic behaviours."
Jam M., Flament D., Allouch J., Potin P., Thion L., Kloareg B., Czjzek M., Helbert W., Michel G., Barbeyron T.
Biochem. J. 385:703-713(2005) [PubMed: 15456406] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Dsij EMBL AAF21820.1.
[2]"The three-dimensional structures of two beta-agarases."
Allouch J., Jam M., Helbert W., Barbeyron T., Kloareg B., Henrissat B., Czjzek M.
J. Biol. Chem. 278:47171-47180(2003) [PubMed: 12970344] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 20-295.
[3]"Parallel substrate binding sites in a beta-agarase suggest a novel mode of action on double-helical agarose."
Allouch J., Helbert W., Henrissat B., Czjzek M.
Structure 12:623-632(2004) [PubMed: 15062085] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 20-290.

Cross-references

Sequence databases

AF098954 Genomic DNA. Translation: AAF21820.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1O4YX-ray1.48A20-295[»]
1URXX-ray1.70A20-290[»]
ModBaseSearch...

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Family and domain databases

InterProIPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PfamPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ9RGX9_9FLAO
AccessionPrimary (citable) accession number: Q9RGX9
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information