\
logo
  Home | Contact us | Browse | Quick Search by UniProtKB ID, Keyword, PDBID

Menu:

Latest news:

Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

Read more...


Protein Name: Oxalate--CoA ligase

UniprotKB/SwissProt ID: Q9SMT7 (Q9SMT7)

Gene Name: AAE3

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Oxalyl-CoA synthetase acting exclusively against oxalate (PubMed:22447686, PubMed:27326693). Follows a two-step reaction mechanism, wherein oxalate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield oxalyl-CoA (By similarity). No activity with malonate, succinate, malate, acetate, formate, lactate, glycolate, glyoxylate or glutarate (PubMed:22447686). Required for oxalate degradation, normal seed development and defense against oxalate-producing fungal pathogens (PubMed:22447686)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR025110 AMP-bd_C
IPR045851 AMP-bd_C_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_synth/lig_dom
IPR042099 ANL_N_sf
IPR045310 Pcs60-like

The S-nitrosylation sites of Q9SMT7

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 364 IQEPNNKGEV C IRGPNVTKGY   
2 455 PDEKYGEEIN C AVIPREGTTV