Q81M95 (ARGC_BACAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 73.
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 | Bacillus anthracis | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 345 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. |
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 – 345 | 345 | N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150 | PRO_0000112377 | |||||
Sites | |||||||||
| Active site | 149 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP28073.1. AE017334 Genomic DNA. Translation: AAT33475.1. AE017225 Genomic DNA. Translation: AAT56341.1. |
| RefSeq | NP_846587.1. NC_003997.3. YP_021000.1. NC_007530.2. YP_030290.1. NC_005945.1. |
3D structure databases | |
| ProteinModelPortal | Q81M95. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000009414; EBBACP00000009170; EBBACG00000009406. EBBACT00000014126; EBBACP00000013747; EBBACG00000014118. EBBACT00000022493; EBBACP00000021978; EBBACG00000022484. |
| GeneID | 1087584. 2816434. 2848270. |
| GenomeReviews | Gene locus BA_4355 in contig AE016879_GR. Gene locus BAS4040 in contig AE017225_GR. Gene locus GBAA_4355 in contig AE017334_GR. |
| KEGG | ban:BA_4355. bar:GBAA_4355. bat:BAS4040. |
| TIGR | BA_4355. GBAA_4355. |
Phylogenomic databases | |
| GeneTree | EBGT00050000002599. |
| HOGENOM | HBG294213. |
| OMA | VCRIAVH. |
| ProtClustDB | PRK00436. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS4040-MONOMER. BANT261594:GBAA4355-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_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81M95 Secondary accession number(s): Q6HTP8, Q6KMY7 | ||||||||
| 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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