Q8NJK5 (RGLA_ASPNG) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 11, 2011.
Version 27.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Rhamnogalacturonate lyase A EC=4.2.2.- | ||
| Gene names |
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| Organism | Aspergillus niger | ||
| Taxonomic identifier | 5061 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 499 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Lyase |
| Gene Ontology (GO) | |
| Biological process | cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | carbohydrate binding Inferred from electronic annotation. Source: InterPro carbon-oxygen lyase activity, acting on polysaccharidesInferred from electronic annotation. Source: InterPro carboxypeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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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 | |
| ProteinModelPortal | Q8NJK5. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | PL4. Polysaccharide Lyase Family 4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR013784. 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] |
| Gene3D | G3DSA:2.60.40.1120. CarboxyPept_regulatory. 1 hit. |
| Pfam | PF09284. RhgB_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF011794. Rhamnogalacturonase_B. 1 hit. |
| SUPFAM | SSF49452. CBD_4. 1 hit. SSF49785. Gal_bind_like. 1 hit. SSF74650. Gal_mut_like. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RGLA_ASPNG | ||||||||
| Accession | Primary (citable) accession number: Q8NJK5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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