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Q8NJK5 (RGLA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 11, 2011. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Rhamnogalacturonate lyase A

EC=4.2.2.-
Gene names
Name:rglA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length499 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin By similarity.

Catalytic activity

Cleaves the alpha-1,4 linkage of RG-I backbone between a rhamnose and a galacturonate, thereby creating an unsaturated bond between carbons 4 and 5 of the galacturonate residue.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the polysaccharide lyase 4 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 499479Rhamnogalacturonate lyase A
PRO_0000394368

Experimental info

Non-terminal residue4991

Sequences

Sequence LengthMass (Da)Tools
Q8NJK5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 0CBD6E4A4EFB0D1E

FASTA49953,915
        10         20         30         40         50         60 
MLSKTSLLSL LSLAAGVVNA DFGITTSDSY VINANSPNSL VFTVDRGSCD ITSIVHYGTE 

        70         80         90        100        110        120 
LQYSGKGSHI GSGLGTATVS ATKSGDYIKV TCETDTLTQY MGVHDGDRII HMATYITEEP 

       130        140        150        160        170        180 
SIGELRFIAR LNSDVLPNEE PFGDVSNTAD GEPIEGSDVF LVDGETRSKF YSSQRFIDDQ 

       190        200        210        220        230        240 
RHCIAGDEHR VCMILNQYET SSGGPFHRDI NSNNGGDYNS LYWYMNSGHV QLESYRMGLH 

       250        260        270        280        290        300 
GPYSMYFSRS GTPSTDIDTS FFADLDIEGY VAESGRGTVS GTASGADSSF DWVVHWYNDD 

       310        320        330        340        350        360 
AQYWTYTSSS GSFTSPAMKP GTYTMVYYQG EYVVATSEVT VSAGSSTSKD ISGSVETGTT 

       370        380        390        400        410        420 
IFKIGDWDGQ PTGFRNAENQ LRMHPSDSRM SDWGPLTYTV GSSSLTDFPM AIFKSVNSPV 

       430        440        450        460        470        480 
TIKFTATSDQ TGAATLRIRT TLSFAGGRPQ ATINDYEGSA PSAPTNLDSR GVTRGAYRGY 

       490 
GDVYDVSVPE GTIVEGENT 

« Hide

References

[1]"Expression profiling of pectinolytic genes from Aspergillus niger."
de Vries R.P., Jansen J., Aguilar G., Paenicova L., Joosten J.A.E., Wulfert F., Visser J.
FEBS Lett. 530:41-47(2002) [PubMed: 12387863] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ489944 Genomic DNA. Translation: CAD36194.1.

3D structure databases

ProteinModelPortalQ8NJK5.
ModBaseSearch...

Protein family/group databases

CAZyPL4. Polysaccharide Lyase Family 4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013784. Carb-bd-like_fold.
IPR014766. CarboxyPept_regulatory_dom.
IPR008979. Galactose-bd-like.
IPR011013. Glyco_hydro-type_carb-bd.
IPR016590. Rhamnogalacturonase_B.
IPR015364. RhgB_N.
[Graphical view]
Gene3DG3DSA:2.60.40.1120. CarboxyPept_regulatory. 1 hit.
PfamPF09284. RhgB_N. 1 hit.
[Graphical view]
PIRSFPIRSF011794. Rhamnogalacturonase_B. 1 hit.
SUPFAMSSF49452. CBD_4. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
SSF74650. Gal_mut_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRGLA_ASPNG
AccessionPrimary (citable) accession number: Q8NJK5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: October 1, 2002
Last modified: January 11, 2011
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families