P65788 (PROA_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 56.
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 |
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| Organism | Mycobacterium tuberculosis | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 415 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. HAMAP MF_00412 |
| Catalytic activity | L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP MF_00412 |
| Pathway | Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP MF_00412 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00412. |
| 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological process | proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Inferred from direct assay. Source: MTBBASE plasma membraneInferred from direct assay. Source: MTBBASE |
| Molecular function | NADP binding Inferred from electronic annotation. Source: InterPro glutamate-5-semialdehyde dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 415 | 415 | Gamma-glutamyl phosphate reductase HAMAP MF_00412 | PRO_0000189753 | |||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842579 Genomic DNA. Translation: CAB03769.1. AE000516 Genomic DNA. Translation: AAK46797.1. |
| PIR | A70679. |
| RefSeq | NP_216943.1. NC_000962.2. NP_336983.1. NC_002755.2. |
3D structure databases | |
| ProteinModelPortal | P65788. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000002819; EBMYCP00000002819; EBMYCG00000002817. EBMYCT00000069611; EBMYCP00000067670; EBMYCG00000069606. |
| GeneID | 885536. 925836. |
| GenomeReviews | Gene locus MT2500 in contig AE000516_GR. Gene locus Rv2427c in contig AL123456_GR. |
| KEGG | mtc:MT2500. mtu:Rv2427c. |
| PATRIC | 18127248. VBIMycTub22151_2732. |
| TIGR | MT2500. |
Organism-specific databases | |
| TubercuList | Rv2427c. |
Phylogenomic databases | |
| GeneTree | EBGT00050000015663. |
| HOGENOM | HBG318080. |
| OMA | QYPAACN. |
| PhylomeDB | P65788. |
| ProtClustDB | PRK00197. |
Family and domain databases | |
| HAMAP | MF_00412. ProA. [Tree] |
| 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] |
| Gene3D | G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 2 hits. |
| KO | K00147. |
| PANTHER | PTHR11063:SF1. GSA_DH. 1 hit. |
| Pfam | PF00171. Aldedh. 2 hits. [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_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P65788 Secondary accession number(s): P71921 | ||||||||
| 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 |

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