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 IDPPepDB_5035
Peptide NameALLN_ALLCE
PMID(s)--NA--
Plant Source (Scientific Name)Allium cepa
Plant Source (Common Name)Onion
Plant FamilyAmaryllidaceae
Peptide Family--NA--
Peptide FunctionSignaling-peptide
Peptide Function DescriptionChloride; 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--
SequenceDETVYNKLLNYMTKNTEGTSRETQLRSLKILKEVIAMVKTQNGTMRDLNTFGFQKLRERWVNITALLDKSDRFSYQKLPQSEYCNYFRRMRPPSPSYAWVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTATPCAPQSKVVAHAPYYPIKGCKSIYYMVYYWPHYTPIKYKADEDIMLFTMSKYTGHSGSRFGWALIKKCEWEEDKDCYQTFQNGRINTQSGEGFEAGSRYVRLSLIKTKDDFDQLMYLFLEEYWQQHKENSAVLVSGWHRMSYFFNPVSNFISFELEKTIKELHEIVMESYDKVGSNKVPCLLILTCIIMSSFVNNNIVQAKVSWSLKAAEEAEAVANINCSGHGRAFLDGILSDGSPKCECNTCYTGADCSEKITGCSADVASGDGVFREQTKYFDKKGYEWKGNAADYVNTSTPEQFIEMVTSPNNPEGLLRHEVYLKIMVEAKRKTPLIKQLSNDQISRRPFI
Sequence Length479
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)54838.59
Monoisotopic Molecular Weight (Da)54803.18
Isoelectric Point (pI)8.4
Method / Extraction--NA--


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_5035


External links (Uniprot, PDB and Source Information Database)
UniprotP31757
NCBI--NA--
EMBLZ12621
Link to Source DatabasesSPdb8011
Addtional InformationCATALYTIC 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.