Q9RZC5 (Q9RZC5_DEIRA) Unreviewed, UniProtKB/TrEMBL
Last modified
May 29, 2013.
Version 74.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Acetylornithine/acetyl-lysine aminotransferase HAMAP-Rule MF_01107 Short name=ACOAT HAMAP-Rule MF_01107 EC=2.6.1.- HAMAP-Rule MF_01107 EC=2.6.1.11 HAMAP-Rule MF_01107 | ||||||
| Gene names |
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| Organism | Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP] EMBL AAF12279.1 | ||||||
| Taxonomic identifier | 243230 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › ![]() |
Protein attributes
| Sequence length | 454 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-Rule MF_01107 |
| Catalytic activity | N(2)-acetyl-L-lysine + 2-oxoglutarate = N-acetyl-L-aminoadipate semialdehyde + L-glutamate. HAMAP-Rule MF_01107 N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP-Rule MF_01107 |
| Cofactor | Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP-Rule MF_01107 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP-Rule MF_01107 Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5. HAMAP-Rule MF_01107 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_01107 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_01107. |
| Sequence similarities | Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. HAMAP-Rule MF_01107 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis HAMAP-Rule MF_01107 Lysine biosynthesis HAMAP-Rule MF_01107 |
| Cellular component | Cytoplasm HAMAP-Rule MF_01107 |
| Ligand | Pyridoxal phosphate HAMAP-Rule MF_01107 SAAS SAAS004636 |
| Molecular function | Aminotransferase HAMAP-Rule MF_01107 SAAS SAAS004636 EMBL AAF12279.1 Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process via aminoadipic acidInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Region | 265 – 268 | 4 | Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107 | ||||||
Sites | |||||||||
| Binding site | 157 | 1 | Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107 | ||||||
| Binding site | 160 | 1 | N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107 | ||||||
| Binding site | 321 | 1 | N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107 | ||||||
| Binding site | 322 | 1 | Pyridoxal phosphate By similarity HAMAP-Rule MF_01107 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 294 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107 | ||||||
Sequences
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References
| [1] | "Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. Fraser C.M.Science 286:1571-1577(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE001825 Genomic DNA. Translation: AAF12279.1. |
| PIR | G75595. |
| RefSeq | NP_285353.1. NC_001264.1. |
3D structure databases | |
| ProteinModelPortal | Q9RZC5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 243230.DR_A0029. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAF12279; AAF12279; DR_A0029. |
| GeneID | 1798195. |
| KEGG | dra:DR_A0029. |
| PATRIC | 21633094. VBIDeiRad64572_2917. |
Phylogenomic databases | |
| HOGENOM | HOG000020206. |
| KO | K00823. |
| OMA | ASKSAYR. |
| ProtClustDB | PRK05769. |
Enzyme and pathway databases | |
| BioCyc | DRAD243230:GH46-2720-MONOMER. |
| UniPathway | UPA00033; UER00038. UPA00068; UER00109. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 2 hits. |
| HAMAP | MF_01107. ArgD_aminotrans_3. |
| InterPro | IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. IPR004636. Trfase_AcOrn/SuccOrn_fam. [Graphical view] |
| PANTHER | PTHR11986. PTHR11986. 1 hit. |
| Pfam | PF00202. Aminotran_3. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| PROSITE | PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q9RZC5_DEIRA | ||||||||
| Accession | Primary (citable) accession number: Q9RZC5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
