Q69RJ0 · GLTB_ORYSJ
- ProteinFerredoxin-dependent glutamate synthase, chloroplastic
- GeneGLU
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1615 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Involved in glutamate biosynthesis in leaf. Required for the reassimilation of ammonium ions generated during photorespiration (By similarity).
Catalytic activity
- 2 oxidized [2Fe-2S]-[ferredoxin] + 2 L-glutamate = L-glutamine + 2 reduced [2Fe-2S]-[ferredoxin] + 2-oxoglutarate + 2 H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [3Fe-4S] cluster.
Pathway
Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin route): step 1/1.
Energy metabolism; nitrogen metabolism.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 97 | Nucleophile | |||
Binding site | 1175-1232 | FMN (UniProtKB | ChEBI) | |||
Binding site | 1228 | [3Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 1234 | [3Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 1239 | [3Fe-4S] cluster (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | 3 iron, 4 sulfur cluster binding | |
Molecular Function | glutamate synthase (ferredoxin) activity | |
Molecular Function | glutamate synthase (NADH) activity | |
Molecular Function | metal ion binding | |
Biological Process | ammonia assimilation cycle | |
Biological Process | glutamate biosynthetic process | |
Biological Process | L-glutamate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFerredoxin-dependent glutamate synthase, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ69RJ0
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | ||
---|---|---|---|---|---|---|
Transit peptide | 1-52 | UniProt | Chloroplast | |||
Chain | PRO_0000395203 | 53-1615 | UniProt | Ferredoxin-dependent glutamate synthase, chloroplastic | ||
Modified residue (large scale data) | 211 | PTMeXchange | Phosphoserine | |||
Modified residue (large scale data) | 1609 | PTMeXchange | Phosphothreonine | |||
Proteomic databases
Expression
Tissue specificity
Expressed in leaf blades and at lower levels in roots.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 97-496 | Glutamine amidotransferase type-2 | |||
Sequence similarities
Belongs to the glutamate synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,615
- Mass (Da)175,044
- Last updated2010-07-13 v2
- MD5 Checksum1D6ABC5BFFC390D794F98448981C6254
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0P0X9Q0 | A0A0P0X9Q0_ORYSJ | Os07g0658400 | 788 | ||
A0A0P0X9S7 | A0A0P0X9S7_ORYSJ | Os07g0658400 | 1040 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 1588 | in Ref. 1; BAF46922 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB024716 EMBL· GenBank· DDBJ | BAF46921.1 EMBL· GenBank· DDBJ | mRNA | ||
AB061357 EMBL· GenBank· DDBJ | BAF46922.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP003833 EMBL· GenBank· DDBJ | BAD30339.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AP005184 EMBL· GenBank· DDBJ | BAD31105.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AP008213 EMBL· GenBank· DDBJ | BAF22434.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AP014963 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |