Q59279 (ARGC_CORGL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 87.
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 reductase Short name=AGPR EC=1.2.1.38 Alternative name(s): N-acetyl-glutamate semialdehyde dehydrogenase Short name=NAGSA dehydrogenase | ||||
| Gene names |
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| Organism | Corynebacterium glutamicum (Brevibacterium flavum) | ||||
| Taxonomic identifier | 1718 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 347 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl 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 |
| Subcellular location | Cytoplasm Probable HAMAP MF_00150. |
| Sequence similarities | Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. |
| Sequence caution | The sequence CAF21405.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | arginine biosynthetic process Inferred 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 – 347 | 347 | N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150 | PRO_0000112400 | |||||
Sites | |||||||||
| Active site | 151 | 1 | By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 14 | 1 | A → T in AAB62245. Ref.1 | ||||||
| Sequence conflict | 14 | 1 | A → T in AAC24812. Ref.2 | ||||||
| Sequence conflict | 21 | 1 | L → I in AAB62245. Ref.1 | ||||||
| Sequence conflict | 21 | 1 | L → I in AAC24812. Ref.2 | ||||||
| Sequence conflict | 25 | 1 | H → Q in AAB62245. Ref.1 | ||||||
| Sequence conflict | 25 | 1 | H → Q in AAC24812. Ref.2 | ||||||
| Sequence conflict | 102 | 1 | C → R in AAB62245. Ref.1 | ||||||
| Sequence conflict | 102 | 1 | C → R in AAC24812. Ref.2 | ||||||
| Sequence conflict | 277 | 1 | L → S in AAB62245. Ref.1 | ||||||
| Sequence conflict | 277 | 1 | L → S in AAC24812. Ref.2 | ||||||
| Sequence conflict | 341 | 1 | P → A in AAB62245. Ref.1 | ||||||
| Sequence conflict | 341 | 1 | P → A in AAC24812. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Chun J.Y., Lee E.J., Cheon C.I., Min K.H., Lee M.-S. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613. |
| [2] | "Molecular cloning of the arginine biosynthetic genes from Corynebacterium glutamicum." Park M.Y., Chun J.Y., Ko S.-Y., Lee M.-S. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613. |
| [3] | "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [4] | "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. Tauch A.J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [5] | "Genes and enzymes of the acetyl cycle of arginine biosynthesis in Corynebacterium glutamicum: enzyme evolution in the early steps of the arginine pathway." Sakanyan V., Petrosyan P., Lecocq M., Boyen A., Legrain C., Demarez M.N., Hallet J.-N., Glansdorff N. Microbiology 142:99-108(1996) [PubMed: 8581175] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-347. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF005242 Genomic DNA. Translation: AAB62245.1. AF049897 Genomic DNA. Translation: AAC24812.1. BA000036 Genomic DNA. Translation: BAB98787.1. BX927152 Genomic DNA. Translation: CAF21405.1. Different initiation. X86157 Genomic DNA. Translation: CAA60096.1. |
| RefSeq | NP_600613.1. NC_003450.3. YP_225681.1. NC_006958.1. |
3D structure databases | |
| ProteinModelPortal | Q59279. |
| SMR | Q59279. Positions 4-347. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1019370. 3344983. |
| GenomeReviews | Gene locus Cgl1394 in contig BA000036_GR. Gene locus cg1580 in contig BX927147_GR. |
| KEGG | cgb:cg1580. cgl:NCgl1340. |
| PATRIC | 21494827. VBICorGlu203724_1363. |
Phylogenomic databases | |
| HOGENOM | HBG294213. |
| OMA | VCRIAVH. |
| PhylomeDB | Q59279. |
| ProtClustDB | PRK00436. |
Enzyme and pathway databases | |
| BioCyc | CGLU196627:CG1580-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00150. ArgC_type1. [Tree] |
| InterPro | IPR023013. AGPR_AS. 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. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARGC_CORGL | ||||||||
| Accession | Primary (citable) accession number: Q59279 Secondary accession number(s): O32353 | ||||||||
| 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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