Detailed Peptide Information
This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking
| Primary Information |
| PPepDB ID | PPepDB_5035 |
| Peptide Name | ALLN_ALLCE |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Allium cepa |
| Plant Source (Common Name) | Onion |
| Plant Family | Amaryllidaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Chloride; Direct protein sequencing; EGF-like domain; Glycoprotein; Lyase; Pyridoxal phosphate; Signal; Vacuole | Alliin lyase precursor (EC 4.4.1.4) (Alliinase) (Cysteine sulphoxide,lyase).Vacuole. |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | DETVYNKLLNYMTKNTEGTSRETQLRSLKILKEVIAMVKTQNGTMRDLNTFGFQKLRERWVNITALLDKSDRFSYQKLPQSEYCNYFRRMRPPSPSYAWVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTATPCAPQSKVVAHAPYYPIKGCKSIYYMVYYWPHYTPIKYKADEDIMLFTMSKYTGHSGSRFGWALIKKCEWEEDKDCYQTFQNGRINTQSGEGFEAGSRYVRLSLIKTKDDFDQLMYLFLEEYWQQHKENSAVLVSGWHRMSYFFNPVSNFISFELEKTIKELHEIVMESYDKVGSNKVPCLLILTCIIMSSFVNNNIVQAKVSWSLKAAEEAEAVANINCSGHGRAFLDGILSDGSPKCECNTCYTGADCSEKITGCSADVASGDGVFREQTKYFDKKGYEWKGNAADYVNTSTPEQFIEMVTSPNNPEGLLRHEVYLKIMVEAKRKTPLIKQLSNDQISRRPFI |
| Sequence Length | 479 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 54838.59 |
| Monoisotopic Molecular Weight (Da) | 54803.18 |
| Isoelectric Point (pI) | 8.4 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
| Uniprot | P31757 |
| NCBI | --NA-- |
| EMBL | Z12621 |
| Link to Source Databases | SPdb8011 |
| Addtional Information | CATALYTIC ACTIVITY:An S-alkyl-L-cysteine S-oxide = an alkyl sulfenate 2-aminoacrylate.COFACTOR:Pyridoxal phosphate.SUBUNIT:Homodimer (By similarity).DOMAIN:The 6 Cys residues of the EGF-like domain are arranged in a disulfide pattern different from the one found in the canonical EGFs. The function of this domain is unclear. It may be a binding site for other proteins or the docking site for a putative alliinase receptor (By similarity).SIMILARITY:Contains 1 EGF-like domain. |