A8M8Q9 (ARGC_CALMQ) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 36.
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: N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase Short name=AGPR EC=1.2.1.- EC=1.2.1.38 Alternative name(s): N-acetyl-glutamate semialdehyde/N-acetyl-aminoadipate semialdehyde dehydrogenase Short name=NAGSA dehydrogenase | ||||||
| Gene names |
| ||||||
| Organism | Caldivirga maquilingensis (strain ATCC 700844 / DSMZ 13496 / JCM 10307 / IC-167) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 397948 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Caldivirga |
Protein attributes
| Sequence length | 354 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Involved in both the arginine and lysine biosynthetic pathways By similarity. HAMAP MF_00150 |
| 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 By similarity HAMAP MF_00150. |
| 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: UniProtKB-KW lysine biosynthetic processInferred 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: EC NAD 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 – 354 | 354 | N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase HAMAP MF_00150 | PRO_1000076727 | |||||
Sites | |||||||||
| Active site | 153 | 1 | By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete sequence of Caldivirga maquilingensis IC-167." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. Richardson P.Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700844 / DSMZ 13496 / JCM 10307 / IC-167. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000852 Genomic DNA. Translation: ABW02128.1. |
| RefSeq | YP_001541118.1. NC_009954.1. |
3D structure databases | |
| ProteinModelPortal | A8M8Q9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A8M8Q9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5708908. |
| GenomeReviews | Gene locus Cmaq_1301 in contig CP000852_GR. |
| KEGG | cma:Cmaq_1301. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG294213. |
| OMA | VYRYPEP. |
| ProtClustDB | PRK00436. |
Enzyme and pathway databases | |
| BioCyc | CMAQ397948:CMAQ_1301-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00150. ArgC_type1. [Tree] |
| InterPro | IPR000706. AGPR_type-1. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00145. |
| Pfam | PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view] |
| SMART | SM00859. Semialdhyde_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01850. ArgC. 1 hit. |
| PROSITE | PS01224. ARGC. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARGC_CALMQ | ||||||||
| Accession | Primary (citable) accession number: A8M8Q9 | ||||||||
| Entry history |
| ||||||||
| 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