Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR022278 is a Phosphoserine aminotransferase.
<p>Phosphoserine aminotransferase (PSAT) is involved in serine biosynthesis [[cite:PUB00060960], [cite:PUB00060961]]. The enzyme catalyses the reversible conversion of 3-phosphohydroxypyruvate to L-phosphoserine. PSAT from Escherichia coli has been shown to be a homodimer of Mr79,000 with a conserved lysine that binds covalently to pyridoxal phosphate (PLP). PSAT is a vitamin B6-dependent enzyme and belongs to the alpha family of PLP enzymes. PSAT is also classified as a member of the aspartate aminotransferase family of PLP enzymes [[cite:PUB00016898]]. According to the structural classification of PLP-dependent enzymes [[cite:PUB00027712]], PSAT belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I), where it is allocated to a separated subclass. The mechanism of action in all these enzymes is similar: PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which, depending on the reaction, is the substrate in four kinds of reactions: transamination (movement of amino groups), racemization (redistribution of enantiomers), decarboxylation (removing COOH groups), and various side-chain reactions depending on the enzyme involved.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity | Catalysis of the reaction: O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. | ||
| Biological process | L-serine biosynthetic process | The chemical reactions and pathways resulting in the formation of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: phosphoserine aminotransferase, chloroplastic-like [Cicer arietinum] gi|502153680|ref|XP_004509428.1| | 26 | ||
| – | Phosphoserine aminotransferase; TAIR: AT2G17630.1 Pyridoxal phosphate (PLP)-dependent transferases superfamily protein; Swiss-Prot: sp|Q9SHP0|SERB2_ARATH Phosphoserine aminotransferase 2, chloroplastic; TrEMBL-Plants: tr|A0A1J7HEK4|A0A1J7HEK4_LUPAN Uncharacterized protein; Found in the gene: LotjaGi2g1v0356200 | 24 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd00611 | CDD | 1 | 50.00 |