ProGP1292 (L-aspartate oxidase)
Home -> ProGPdb -> Search ProGP -> Display data
| ProGP ID | ProGP1292 (L-aspartate oxidase) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Haloferax volcanii DS2 |
| Domain | Archaea |
| Classification | Phylum : Euryarchaeota Class : Halobacteria Orders : Haloferacales Family : Haloferacaceae Genus : Haloferax Species : volcanii Strain : DS2 |
| Taxonomic ID (NCBI) | 2246 |
| Genome Information | |
| GenBank | M62816 |
| EMBL | M62816 |
| Organism Additional Information | It is an easily culturable moderate halophile |
| Gene Information | |
| Gene Name | HVO_2580 |
| Protein Information | |
| Protein Name | L-aspartate oxidase |
| UniProtKB/SwissProt ID | D4GU13 |
| UniProtKB Sequence | >tr|D4GU13|D4GU13_HALVD L-aspartate oxidase OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=nadB PE=3 SV=1 MKADVLVVGSGIAGCAAALAAAREGADVLVVTKATEPEDAASDWAQGGIAVTQSAPEEFAADIRRASDGTADPEAVETLVSESRAVVEDVLLDTLGVAFDAVGEGTDADAEASADTDTNSFDLAREAGHSSRRILHVDASTGAHVLRPFLQHLSARDGVRIVEDATALDLLTEEGTVRGATVLADGEVEPVFAGATVLATGGIGDCYARSTNPAGATGDGVAMAALAGATVSDMQYVQFHPTAYDPRTDPRADDDAQPFLVSEAVRGEGAVLRDADGRRFMPDVHDDAELAPRDVVARAVSRARDRSGRVVLDVSDLDFRDEFPDLAALCDDRGVDLDAGIPVAPSEHFLCGGVAVDDRGRASLPRLFAAGECARTGVHGANRLASTSLLEGLVWGVRAGETAADRGRDEAETVEYAPPRDSDPALPDAFADAKFDRLGRTMDELVGIERTPDGLDTARARLRRLKGEVDAYARTRVSRSVYELRNACVSSLLVARAAADAPSAGCHSLVDPDGRDGGDGSDGSDDAGRGVTPSADD |
| Subcellular Location | Sec pathway |
| Function | signal peptidase I |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser/Thr) linked |
| Technique(s) used for Glycosylation Detection | UPLC coupled via a nanospray source to a Q-Exactive HFX tandem MS |
| Glycan Information | |
| Technique(s) used for Glycan Identification | UPLC coupled via a nanospray source to a Q-Exactive HFX tandem MS |
| Protein Glycosylation linked (PGL) gene(s) | |
| Additional Comment | Glycosylation is predicted by glycoproteomic in-silico analysis of raw experimental data available on PRIDE and jPOST. |
| Literature | |
| Year of Identification | 2021 |
| Reference | Schulze, S., Pfeiffer, F., Garcia, B.A. and Pohlschroder, M., 2021. Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea. PLoS biology, 19(6), p.e3001277. |
| Corresponding Author | Mechthild Pohlschroder |
| Contact | Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America |