P55037 (GLTB_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ferredoxin-dependent glutamate synthase 1 EC=1.4.7.1 Alternative name(s): Fd-GOGAT | ||||
| Gene names |
| ||||
| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 1111708 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › ![]() |
Protein attributes
| Sequence length | 1550 AA. |
| Sequence status | Complete. |
| 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 | |
| Sequence similarities | Belongs to the glutamate synthase family. Contains 1 glutamine amidotransferase type-2 domain. |
| Caution | It is uncertain whether Met-1 or Met-21 is the initiator. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Glutamate biosynthesis |
| Domain | Glutamine amidotransferase |
| Ligand | 3Fe-4S FAD FMN Flavoprotein Iron Iron-sulfur Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | L-glutamate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate synthase (ferredoxin) activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| trxA | P52231 | 2 | EBI-862093,EBI-862916 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1550 | 1550 | Ferredoxin-dependent glutamate synthase 1 | PRO_0000170793 | |||||
Regions | |||||||||
| Domain | 43 – 440 | 398 | Glutamine amidotransferase type-2 | ||||||
| Nucleotide binding | 1097 – 1154 | 58 | FMN By similarity | ||||||
Sites | |||||||||
| Active site | 43 | 1 | For GATase activity By similarity | ||||||
| Metal binding | 1150 | 1 | Iron-sulfur (3Fe-4S) By similarity | ||||||
| Metal binding | 1156 | 1 | Iron-sulfur (3Fe-4S) By similarity | ||||||
| Metal binding | 1161 | 1 | Iron-sulfur (3Fe-4S) By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Existence of two ferredoxin-glutamate synthases in the cyanobacterium Synechocystis sp. PCC 6803. Isolation and insertional inactivation of gltB and gltS genes." Navarro F., Chavez S., Candau P., Florencio F.J. Plant Mol. Biol. 27:753-767(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X80485 Genomic DNA. Translation: CAA56652.1. BA000022 Genomic DNA. Translation: BAA17018.1. |
| PIR | S60228. |
| RefSeq | NP_440338.1. NC_000911.1. YP_005650395.1. NC_017277.1. YP_007450221.1. NC_020286.1. |
3D structure databases | |
| ProteinModelPortal | P55037. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P55037. 3 interactions. |
| STRING | 1148.sll1502. |
Proteomic databases | |
| PaxDb | P55037. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAA17018; BAA17018; BAA17018. |
| GeneID | 12256085. 14615869. 953637. |
| KEGG | syn:sll1502. syy:SYNGTS_0442. |
| PATRIC | 23837822. VBISynSp132158_0480. |
Phylogenomic databases | |
| eggNOG | COG0069. |
| HOGENOM | HOG000031559. |
| KO | K00284. |
| OMA | WMAARQA. |
| ProtClustDB | CLSK892635. |
Enzyme and pathway databases | |
| UniPathway | UPA00045. UPA00634; UER00691. |
Family and domain databases | |
| Gene3D | 2.160.20.60. 1 hit. 3.20.20.70. 2 hits. |
| InterPro | IPR013785. Aldolase_TIM. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR002489. Glu_synth_asu_C. IPR002932. Glu_synth_centr_C. IPR006982. Glu_synth_centr_N. [Graphical view] |
| Pfam | PF00310. GATase_2. 1 hit. PF04898. Glu_syn_central. 1 hit. PF01645. Glu_synthase. 1 hit. PF01493. GXGXG. 1 hit. [Graphical view] |
| SUPFAM | SSF69336. Glu_synthase_C. 1 hit. |
| PROSITE | PS51278. GATASE_TYPE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLTB_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: P55037 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
