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_4119 |
| Peptide Name | GWD2_ARATH |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Arabidopsis thaliana |
| Plant Source (Common Name) | Mouse-ear cress |
| Plant Family | Brassicaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Signal; Transferase | Alpha-glucan water dikinase 2 precursor (EC 2.7.9.4). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | ADLESAIDTFLSPSKGHHVFAVNGLSPKLQDLLNLVKRLVREENTEPLIEALRNELITKLRSERMPYLGDESGWNRSWVAIKKVWASKWNERAYVSCKKNAVLDRLQLVLADRCQHYFTIIQPTAKYLGQLLRVDKHGIDVFTEEVIRAGCFDQNVLSNLKSKEGRAISIHTKSTGLVISDGNNSDVSVRHIFISSVPRGDGSHNRWLRQHNGNFRVEIPWNDLHAHHRIPKTLIERRAHKIWDRKGRPQDVLPEKSKFVHGACQTQFTDMSSREHSYQFIDINLKRGGFVGIQFVIWSGEGNAGAGLYDSVIMDEAEEVVVDYSREPLIMDKSFRVRLFSAIAEAGNVIESIYGCPQDIEGVVKGGHIYIVQARPQVFHVRNYEITVLQRDVKGDCRLWIATNMAGPTVLHWGVAKSSAGEWLIPPPGYWVNNNGANFVVNLKSADSTSGKLDVDEKYVLKWLLDEISEREKEAERSIQSYRRKHDVQKWLQKYTEPINRSGSVKSSALAELSKRSVGQENLVSQKSISEALERFTNLMEKIYLQQPNKREIVRLTMALVGRGGQGDVGQRIRDEILKLDHDAVCMAVLIQEVICGDYAFVIHTNNPVSGDSSEIYTEIVKGLGETLKLVDARIQLHPALRAPRTRAKDLLFLDIALESCFKTTIEKRLISLNFNNPLMHRFNIATELTERCKDEGEGGCIGIMVWMRFMATRHLTWNKNYNVKPREMATSKSQQFQLIEGMELQITVTGLPNGSSVRAEFHLKNCTRAWILHWGCIPEIIYVICVVLENLCLSIVNNEEIIFCTKDWYRVSEAYRPHDVQWALQTKPFGTFENILSDDSNKDVARRISVLKDSLNRGDLTKLKSIQEAILQMSAPMPGAVLSTLVNRFDPSLRKIANLGCWQVISSADAYGFVVCVNELIVVQNKFSSAREQQIDYDNAVRELHAELARGISLDELQANSTVPVEKEETSEPHHTMTLQTNGLTKERLASYDRPIVSEPRFRSDSKEGLIRDLTMYLKTLKAVHSGVGAYPGRAMSFITKKTNLKSPTVISYPSKRIGLYSKPSIIFRSDSNNEDLVIQRNNHCKSGMMEEWHQKLHNNSSADDVIICEALLNYVRSDFRIDAYWQVISKGKKFCGHYVISSKEFTDERVGSKSYNIKFLRERVPSWIKIPTSAALYQGNNHWYIPSEHSSKQGALQTTFVKSGDAYVVILELRDPRVRAIEFVLKYSKPTVIIASKVTGEEEIPAGVVAVLTPSMIDVLSHVSIRARNSKACFAT |
| Sequence Length | 1278 |
| Validation | Experimental evidence at transcript level |
| Average Molecular Weight (Da) | 144769.67 |
| Monoisotopic Molecular Weight (Da) | 144678.74 |
| Isoelectric Point (pI) | 8.75 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | Q9STV0 |
| NCBI | --NA-- |
| EMBL | AL078637 |
| Link to Source Databases | SPdb105489 |
|---|
| Addtional Information | FUNCTION:Mediates the incorporation of phosphate into alpha- glucan, mostly at the C-6 position of glucose units (By similarity).CATALYTIC ACTIVITY:ATP alpha-glucan H(2)O = AMP phospho- alpha-glucan phosphate.COFACTOR:Magnesium (By similarity).SUBUNIT:Homodimer (By similarity).DOMAIN:The N-terminal domain contains the alpha-glucan binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the ATP binding site (By similarity).MISCELLANEOUS:The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the C-terminal domain, and the third partial reaction is catalyzed at an active site located on the N- terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the C-terminal domain to that of the B-terminal domain (By similarity).SIMILARITY:Belongs to the PEP-utilizing enzyme family.SEQUENCE CAUTION:Sequence=CAB45080.1; Type=Erroneous gene model prediction; Sequence=CAB79355.1; Type=Erroneous gene model prediction; |
