Gene: EL10Ac2g04056
General Information
Structural Information
- Species Beta vulgaris
- Gene Identifier EL10Ac2g04056
- Transcript Identifier EL10Ac2g04056.1
- Gene Type Coding gene
- Location Chr2_EL10_PGA_scaffold6 : 44193795-44196774 : negative
Gene Family Information
- ID HOM05D000658
- #Genes/#Species 864/100
- Phylogenetic origin
- ID ORTHO05D003223
- #Genes/#Species 237/99
- Phylogenetic origin
Gene Duplication Information
Labels
Identifiers
- id EL10Ac2g04056.EL10_1.0
- pacid 43407487
Descriptions
- Description 4.1.3.38 - Aminodeoxychorismate lyase / Enzyme X
- Loading (ortholog descriptions from ath)...
Functional Annotation
Biological Process
GO term | Evidence(s) | Provider(s) | Description | Source(s) |
---|---|---|---|---|
GO:0008153 | ISO | PLAZA Integrative Orthology | para-aminobenzoic acid biosynthetic process | AT5G57850 |
GO:0006520 | ISO | PLAZA Homology (enrichment) | cellular amino acid metabolic process | HOM05D000658 |
GO:0046654 | ISO | PLAZA Integrative Orthology | tetrahydrofolate biosynthetic process | AT5G57850 |
GO:0009058 | ISO | PLAZA Homology (enrichment) | biosynthetic process | HOM05D000658 |
Molecular Function
GO term | Evidence(s) | Provider(s) | Description | Source(s) |
---|---|---|---|---|
GO:0003824 | IEA | InterPro | catalytic activity | |
GO:0030170 | ISO | PLAZA Homology (enrichment) | pyridoxal phosphate binding | HOM05D000658 |
GO:0008483 | ISO | PLAZA Homology (enrichment) | transaminase activity | HOM05D000658 |
GO:0008696 | ISO | PLAZA Integrative Orthology | 4-amino-4-deoxychorismate lyase activity | AT5G57850 |
Cellular Component
GO term | Evidence(s) | Provider(s) | Description | Source(s) |
---|---|---|---|---|
GO:0009570 | ISO | PLAZA Integrative Orthology | chloroplast stroma | AT5G57850 |
GO:0009507 | ISO | PLAZA Integrative Orthology | chloroplast | AT5G57850 |
Color Legend
Experimental Evidence |
Computational Reviewed Evidence |
Electronic Evidence |
Mapman id | Description |
---|---|
7.5.1.2 | Coenzyme metabolism.tetrahydrofolate metabolism.p-aminobenzoate biosynthesis.aminodeoxychorismate lyase |