Basic Information
Gene ID
Position
hic_scaffold_21:69495393-69498295 (-)
2902bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family
Organism
Also AS AT3G08860

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
PH02Gene48692 Acyl-CoA dehydrogenase, N-terminal domain
PH02Gene51355 Cys/Met metabolism PLP-dependent enzyme
PH02Gene50268 Interconversion of serine and glycine
Regulatory gene
PH02Gene00452 DNA-binding domain in plant proteins such as APETALA2 and EREBPs
PH02Gene01001 ethylene-responsive transcription factor
PH02Gene01037 DNA-binding domain in plant proteins such as APETALA2 and EREBPs

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
GO Term Description GO Category
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0005488 binding MF
GO:0005515 protein binding MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005739 mitochondrion CC
GO:0007154 cell communication BP
GO:0008144 obsolete drug binding MF
GO:0008150 biological_process BP
GO:0008453 alanine-glyoxylate transaminase activity MF
GO:0008483 transaminase activity MF
GO:0009605 response to external stimulus BP
GO:0009987 cellular process BP
GO:0009991 response to extracellular stimulus BP
GO:0016740 transferase activity MF
GO:0016769 transferase activity, transferring nitrogenous groups MF
GO:0019842 vitamin binding MF
GO:0030170 pyridoxal phosphate binding MF
GO:0031667 response to nutrient levels BP
GO:0031668 cellular response to extracellular stimulus BP
GO:0031669 cellular response to nutrient levels BP
GO:0036094 small molecule binding MF
GO:0042802 identical protein binding MF
GO:0043167 ion binding MF
GO:0043168 anion binding MF
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043562 cellular response to nitrogen levels BP
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0048037 obsolete cofactor binding MF
GO:0050662 obsolete coenzyme binding MF
GO:0050896 response to stimulus BP
GO:0051716 cellular response to stimulus BP
GO:0070279 vitamin B6 binding MF
GO:0071496 cellular response to external stimulus BP
GO:0097159 organic cyclic compound binding MF
GO:1901363 heterocyclic compound binding MF
KEGG Term Name Description
map01110 Biosynthesis of secondary metabolites -
map01100 Metabolic pathways -
map00280 Valine, leucine and isoleucine degradation -
map00270 Cysteine and methionine metabolism Cysteine and methionine are sulfur-containing amino acids. Cysteine is synthesized from serine through different pathways in different organism groups. In bacteria and plants, cysteine is converted from serine (via acetylserine) by transfer of hydrogen sulfide [MD:M00021]. In animals, methionine-derived homocysteine is used as sulfur source and its condensation product with serine (cystathionine) is converted to cysteine [MD:M00338]. Cysteine is metabolized to pyruvate in multiple routes. Methionine is an essential amino acid, which animals cannot synthesize. In bacteria and plants, methionine is synthesized from aspartate [MD:M00017]. S-Adenosylmethionine (SAM), synthesized from methionine and ATP, is a methyl group donor in many important transfer reactions including DNA methylation for regulation of gene expression. SAM may also be used to regenerate methionine in the methionine salvage pathway [MD:M00034].
map00260 Glycine, serine and threonine metabolism Serine is derived from 3-phospho-D-glycerate, an intermediate of glycolysis [MD:M00020], and glycine is derived from serine. Threonine is an essential amino acid, which animals cannot synthesize. In bacteria and plants, threonine is derived from aspartate [MD:M00018].
map00250 Alanine, aspartate and glutamate metabolism -