Reviewed,
UniProtKB/Swiss-Prot O50146 (ARGC2_THET2)
Last modified
June 16, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase Short name=AGPR EC=1.2.1.38 EC=1.2.1.- Alternative name(s): N-acetyl-glutamate semialdehyde/N-acetyl-aminoadipate semialdehyde dehydrogenase Short name=NAGSA dehydrogenase | ||||||
| Gene names |
| ||||||
| Organism | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 262724 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 344 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Involved in both the arginine and lysine biosynthetic pathways By similarity. |
| Catalytic activity | N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. HAMAP MF_00150 N(2)-acetyl-L-aminoadipate-semialdehyde + NADP+ + phosphate = N(2)-acetyl-L-gamma-aminoadipyl phosphate + NADPH. HAMAP MF_00150 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. HAMAP MF_00150 Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5. HAMAP MF_00150 |
| Subcellular location | Cytoplasm Probable. |
| Sequence similarities | Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis Lysine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: HAMAP NAD or NADH bindingInferred from electronic annotation. Source: InterPro protein dimerization activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 344 | 344 | N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase HAMAP MF_00150 | PRO_0000112501 | |||||
Sites | |||||||||
| Active site | 148 | 1 | By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid." Kobashi N., Nishiyama M., Tanokura M. J. Bacteriol. 181:1713-1718(1999) [PubMed: 10074061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236. |
| [3] | "Molecular cloning and sequence analysis of the lysR gene from the extremely thermophilic eubacterium, Thermus thermophilus HB27." Kosuge T., Hoshino T. FEMS Microbiol. Lett. 157:73-79(1997) [PubMed: 9418242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-344. |
Cross-references
Sequence databases | |
|---|---|
| AE017221 Genomic DNA. Translation: AAS81884.1. AB017109 mRNA. Translation: BAA74767.1. AB006681 Genomic DNA. Translation: BAA23878.1. Different initiation. | |
| PIR | T43947. |
| RefSeq | YP_005511.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2776302. |
| GenomeReviews | Gene locus TT_C1542 in contig AE017221_GR. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O50146. |
| OMA | O50146. GCNATAT. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MON-6802. TTHE262724:TT_C1542-MON. |
Family and domain databases | |
| HAMAP | MF_00150. [Tree] |
| InterPro | IPR000706. AGPR_act_site. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_C. [Graphical view] |
| Pfam | PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view] |
| ProDom | PD003765. AGPR_act_site. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01850. argC. 1 hit. |
| PROSITE | PS01224. ARGC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARGC2_THET2 | ||||||||
| Accession | Primary (citable) accession number: O50146 Secondary accession number(s): Q9ZND6 | ||||||||
| Entry history |
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| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with


