Reviewed,
UniProtKB/Swiss-Prot Q08258 (GLTB_HORVU)
Last modified
June 16, 2009.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ferredoxin-dependent glutamate synthase EC=1.4.7.1 Alternative name(s): FD-GOGAT |
| Organism | Hordeum vulgare (Barley) |
| Taxonomic identifier | 4513 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum |
Protein attributes
| Sequence length | 436 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+. |
| Cofactor | Binds 1 3Fe-4S cluster. FAD. FMN. |
| Pathway | |
| Subunit structure | Monomer. |
| Subcellular location | |
| Sequence similarities | Belongs to the glutamate synthase family. Contains 1 glutamine amidotransferase type-2 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Glutamate biosynthesis |
| Cellular component | Chloroplast Plastid |
| Domain | Glutamine amidotransferase |
| Ligand | 3Fe-4S FAD FMN Flavoprotein Iron Iron-sulfur Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | glutamate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate synthase (ferredoxin) activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›436 | ›436 | Ferredoxin-dependent glutamate synthase | PRO_0000170795 | ||||
Regions | ||||||||
| Domain | 1 – 400 | 400 | Glutamine amidotransferase type-2 | |||||
Sites | ||||||||
| Active site | 1 | 1 | For GATase activity By similarity | |||||
Experimental info | ||||||||
| Non-terminal residue | 436 | 1 | ||||||
Sequences
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References
| [1] | "Cloning and sequence analysis of a cDNA for barley ferredoxin-dependent glutamate synthase and molecular analysis of photorespiratory mutants deficient in the enzyme." Avila C., Marquez A.J., Pajuelo P., Cannell M.E., Wallsgrove R.M., Forde B.G. Planta 189:475-483(1993) [PubMed: 7763576] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-436, PARTIAL PROTEIN SEQUENCE. Strain: cv. Maris Mink. |
Cross-references
Sequence databases | |
|---|---|
| S58774 mRNA. Translation: AAC60547.1. | |
| PIR | T06210. |
| UniGene | Hv.25558 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LM1 based on UniProtKB P55038. |
| ModBase | Search... |
Organism-specific databases | |
| Gramene | Q08258. |
Enzyme and pathway databases | |
| BRENDA | 1.4.7.1. 283. |
Family and domain databases | |
| InterPro | IPR000583. GATase_2. IPR017932. GATase_II. [Graphical view] |
| Pfam | PF00310. GATase_2. 1 hit. [Graphical view] |
| PROSITE | PS51278. GATASE_TYPE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLTB_HORVU | ||||||||
| Accession | Primary (citable) accession number: Q08258 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


