A8G3V6 (PROA_PROM2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 48.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Gamma-glutamyl phosphate reductase Short name=GPR EC=1.2.1.41 Alternative name(s): Glutamate-5-semialdehyde dehydrogenase Glutamyl-gamma-semialdehyde dehydrogenase Short name=GSA dehydrogenase | ||||
| Gene names |
| ||||
| Organism | Prochlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 93060 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Prochlorales › Prochlorococcaceae › Prochlorococcus › ![]() |
Protein attributes
| Sequence length | 436 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate By similarity. HAMAP-Rule MF_00412 |
| Catalytic activity | L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP-Rule MF_00412 |
| Pathway | Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP-Rule MF_00412 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the gamma-glutamyl phosphate reductase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Proline biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | NADP binding Inferred from electronic annotation. Source: InterPro glutamate-5-semialdehyde dehydrogenase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 436 | 436 | Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412 | PRO_1000060843 | |||
Sequences
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References
| [1] | "Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MIT 9215. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000825 Genomic DNA. Translation: ABV50287.1. |
| RefSeq | YP_001483873.1. NC_009840.1. |
3D structure databases | |
| ProteinModelPortal | A8G3V6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 93060.P9215_06721. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABV50287; ABV50287; P9215_06721. |
| GeneID | 5614732. |
| KEGG | pmh:P9215_06721. |
| PATRIC | 22990808. VBIProMar119824_0679. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0014. |
| HOGENOM | HOG000246356. |
| KO | K00147. |
| OMA | EVGISTQ. |
| ProtClustDB | PRK00197. |
Enzyme and pathway databases | |
| BioCyc | PMAR93060:GI08-719-MONOMER. |
| UniPathway | UPA00098; UER00360. |
Family and domain databases | |
| Gene3D | 3.40.309.10. 1 hit. 3.40.605.10. 2 hits. |
| HAMAP | MF_00412. ProA. |
| InterPro | IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR000965. G-glutamylP_reductase. IPR020593. G-glutamylP_reductase_CS. IPR012134. Glu-5-SA_DH. [Graphical view] |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| PIRSF | PIRSF000151. GPR. 1 hit. |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| TIGRFAMs | TIGR00407. proA. 1 hit. |
| PROSITE | PS01223. PROA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PROA_PROM2 | ||||||||
| Accession | Primary (citable) accession number: A8G3V6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
