Reviewed,
UniProtKB/Swiss-Prot P53000 (PROA_CAMJE)
Last modified
November 25, 2008.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names 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 | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 410 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH. |
| Pathway | |
| Subcellular location | CytoplasmBy 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 | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: HAMAP |
| 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 – 410 | 410 | Gamma-glutamyl phosphate reductase | PRO_0000189710 | |||||
Experimental info | |||||||||
| Sequence conflict | 57 | 1 | A → K in AAA23030. Ref.1 | ||||||
| Sequence conflict | 100 | 1 | S → N in AAA23030. Ref.1 | ||||||
| Sequence conflict | 104 | 1 | M → I in AAA23030. Ref.1 | ||||||
| Sequence conflict | 283 | 1 | A → T in AAA23030. Ref.1 | ||||||
| Sequence conflict | 293 | 1 | K → E in AAA23030. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of the gamma-glutamyl phosphate reductase gene of Campylobacter jejuni." Louie H., Chan V.L. Mol. Gen. Genet. 240:29-35(1993) [PubMed: 8341262] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43431 / TGH 9011 / Serotype O:3. |
| [2] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
Cross-references
Sequence databases | |
|---|---|
| M74579 Genomic DNA. Translation: AAA23030.1. AL111168 Genomic DNA. Translation: CAL34704.1. | |
| PIR | F81402. S35213. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1O20 based on UniProtKB Q9WYC9. |
| ModBase | Search... |
Genome annotation databases | |
| GenomeReviews | Gene locus Cj0558c in contig AL111168_GR. |
| KEGG | cje:Cj0558c. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P53000. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ0558C-MON. |
Family and domain databases | |
| HAMAP | MF_00412. [Tree] |
| InterPro | IPR016163. Ald_DHase_C. IPR016162. Ald_DHase_N. IPR000965. Gglut_pp_reduct. IPR012134. Glu-5-SA_DHase. [Graphical view] |
| Gene3D | G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| PIRSF | PIRSF000151. GPR. 1 hit. |
| TIGRFAMs | TIGR00407. proA. 1 hit. |
| PROSITE | PS01223. PROA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PROA_CAMJE | ||||||||
| Accession | Primary (citable) accession number: P53000 Secondary accession number(s): Q0PAV8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


