Reviewed,
UniProtKB/Swiss-Prot Q8X4S6 (ARGD_ECO57)
Last modified
November 3, 2009.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acetylornithine/succinyldiaminopimelate aminotransferase Short name=ACOAT Short name=Succinyldiaminopimelate transferase Short name=DapATase EC=2.6.1.11 EC=2.6.1.17 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83334 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 406 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Involved in both the arginine and lysine biosynthetic pathways By similarity. |
| Catalytic activity | N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107 N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate. HAMAP MF_01107 |
| Cofactor | Binds 1 pyridoxal phosphate per subunit By similarity. |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107 Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 2/3. HAMAP MF_01107 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm Probable. |
| Miscellaneous | The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine By similarity. |
| Sequence similarities | Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis Lysine 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: HAMAP lysine biosynthetic processInferred 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: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro succinyldiaminopimelate transaminase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 406 | 405 | Acetylornithine/succinyldiaminopimelate aminotransferase HAMAP MF_01107 | PRO_0000112745 | |||||
Regions | |||||||||
| Region | 108 – 109 | 2 | Pyridoxal phosphate binding By similarity | ||||||
| Region | 226 – 229 | 4 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 141 | 1 | Pyridoxal phosphate; via carbonyl oxygen By similarity | ||||||
| Binding site | 144 | 1 | N(2)-acetyl-L-ornithine By similarity | ||||||
| Binding site | 283 | 1 | N(2)-acetyl-L-ornithine By similarity | ||||||
| Binding site | 284 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 255 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG58467.1. BA000007 Genomic DNA. Translation: BAB37633.1. | |
| PIR | B91155. G86000. |
| RefSeq | NP_289907.1. NP_312237.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QJ3 based on UniProtKB P12995. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 915934. 961532. |
| GenomeReviews | Gene locus Z4720 in contig AE005174_GR. Gene locus ECs4210 in contig BA000007_GR. |
| KEGG | ece:Z4720. ecs:ECs4210. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8X4S6. |
| OMA | ERTRVIT. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS4210-MON. |
Family and domain databases | |
| HAMAP | MF_01107. [Tree] |
| InterPro | IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR017652. SuccinylOrn_transaminase. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| PANTHER | PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit. |
| Pfam | PF00202. Aminotran_3. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03246. arg_catab_astC. 1 hit. TIGR00707. argD. 1 hit. |
| PROSITE | PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARGD_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8X4S6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


