Q9FNK4 · OAT_ARATH
- ProteinOrnithine aminotransferase, mitochondrial
- GeneDELTA-OAT
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids475 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mediates degradation of arginine for nitrogen recycling. Plays a role in non-host disease resistance by regulating pyrroline-5-carboxylate metabolism-induced hypersensitive response.
Catalytic activity
- a 2-oxocarboxylate + L-ornithine = L-glutamate 5-semialdehyde + an L-alpha-amino acid
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
91 mM | L-ornithine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
28 μmol/h/mg | toward L-glutamate 5-semialdehyde |
The activity was enhanced in young plants under salt-stress conditions.
Pathway
Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 142-143 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 177 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 180 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 265-268 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DEVQ | ||||||
Binding site | 323 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 324 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | plastid | |
Molecular Function | ornithine aminotransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | zinc ion binding | |
Biological Process | arginine catabolic process to glutamate | |
Biological Process | defense response to bacterium | |
Biological Process | hyperosmotic salinity response | |
Biological Process | mitochondrion localization | |
Biological Process | ornithine catabolic process | |
Biological Process | plant-type hypersensitive response | |
Biological Process | proline biosynthetic process | |
Biological Process | response to salt stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOrnithine aminotransferase, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9FNK4
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Unable to use arginine or ornithine as nitrogen source. Displays sensitivity against type II non-host pathogen infection.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 47 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-16 | Mitochondrion | ||||
Sequence: MAATTRRLLYYVSKRF | ||||||
Chain | PRO_0000421298 | 17-475 | Ornithine aminotransferase, mitochondrial | |||
Sequence: STAGVRRSYGGLPQSNSKSPPSSSQRLMELESEFSAHNYHPVPVVFSRANGSTIWDPEGKRYIDFLAAYSAVNQGHCHPKIMKALQEQVEKLTLSSRAFYNDKFPVFAERLTNMFGYDMVLPMNTGAEGVETALKLARKWGHEKKNIPKDEAIIVSCCGCFHGRTLAIVSMSCDNDATRGFGPLLPGNLKVDFGDADSLEKIFKEKGDRIAGFLFEPIQGEAGVIIPPDGYLKAVRELCTKYNVLMIADEVQSGLARSGKMLACDWEEIRPDMVILGKALGGGVIPVSAVLADKDVMLHIKPGQHGSTFGGNPLASAVAMASLDVIVEEKLVERSASLGEELRIQLNEIKKQFPKYIKEVRGRGLFNAIEFNSESLSPVSAYDICLSLKERGVLAKPTHNTIVRLTPPLSISSDELRDGSEALHDVLELDLPNLLKINSGKTPVSHITECDRCGRNLYA | ||||||
Modified residue | 294 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
PTM databases
Expression
Induction
By salt stress in young plants. Up-regulated during low water potential. Induced upon non-host pathogen infection.
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 23-43 | Disordered | ||||
Sequence: RSYGGLPQSNSKSPPSSSQRL | ||||||
Compositional bias | 24-43 | Polar residues | ||||
Sequence: SYGGLPQSNSKSPPSSSQRL |
Sequence similarities
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length475
- Mass (Da)52,178
- Last updated2001-03-01 v1
- ChecksumA886C999AB0B68CC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 24-43 | Polar residues | ||||
Sequence: SYGGLPQSNSKSPPSSSQRL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB006698 EMBL· GenBank· DDBJ | BAB08263.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED95350.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT023421 EMBL· GenBank· DDBJ | AAY56412.1 EMBL· GenBank· DDBJ | mRNA | ||
BT029160 EMBL· GenBank· DDBJ | ABJ17095.1 EMBL· GenBank· DDBJ | mRNA |