P63567 (ARGD_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 52.
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: Acetylornithine aminotransferase Short name=ACOAT EC=2.6.1.11 | ||||
| Gene names |
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| Organism | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 204722 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 403 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107 |
| Cofactor | Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_01107 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01107 |
| Subcellular location | Cytoplasm Probable HAMAP MF_01107. |
| Miscellaneous | May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis. HAMAP MF_01107 |
| Sequence similarities | Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase Transferase |
| Technical term | Complete 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 | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred 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 – 403 | 403 | Acetylornithine aminotransferase HAMAP MF_01107 | PRO_0000112733 | |||||
Regions | |||||||||
| Region | 219 – 222 | 4 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 134 | 1 | Pyridoxal phosphate; via carbonyl oxygen By similarity | ||||||
| Binding site | 137 | 1 | N2-acetyl-L-ornithine By similarity | ||||||
| Binding site | 276 | 1 | N2-acetyl-L-ornithine By similarity | ||||||
| Binding site | 277 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 248 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [2] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014291 Genomic DNA. Translation: AAN29250.1. CP002997 Genomic DNA. Translation: AEM17663.1. |
| RefSeq | NP_697335.1. NC_004310.3. |
3D structure databases | |
| ProteinModelPortal | P63567. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1165962. |
| GenomeReviews | Gene locus BR0301 in contig AE014291_GR. |
| KEGG | bms:BR0301. |
| PATRIC | 17788891. VBIBruSui107850_0314. |
| TIGR | BR0301. |
Phylogenomic databases | |
| HOGENOM | HBG725944. |
| OMA | GRKLWHI. |
| PhylomeDB | P63567. |
| ProtClustDB | PRK01278. |
Enzyme and pathway databases | |
| BioCyc | BSUI204722:BR_0301-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01107. ArgD_aminotrans_3. [Tree] |
| InterPro | IPR004636. AcOrn/SuccinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits. |
| KO | K00821. |
| PANTHER | PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit. |
| Pfam | PF00202. Aminotran_3. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| TIGRFAMs | TIGR00707. ArgD. 1 hit. |
| PROSITE | PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARGD_BRUSU | ||||||||
| Accession | Primary (citable) accession number: P63567 Secondary accession number(s): G0K657, Q8YFA1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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