A7ZML6 (ASTC_ECO24) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 33.
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: Succinylornithine transaminase EC=2.6.1.81 Alternative name(s): Succinylornithine aminotransferase | ||||||
| Gene names |
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| Organism | Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 331111 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 406 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase By similarity. HAMAP MF_01173 |
| Catalytic activity | N(2)-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01173 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP MF_01173 |
| Pathway | Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. HAMAP MF_01173 |
| Sequence similarities | Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Arginine metabolism |
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro succinylornithine 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 406 | 406 | Succinylornithine transaminase HAMAP MF_01173 | PRO_1000164373 | |||||
Amino acid modifications | |||||||||
| Modified residue | 252 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E24377A / ETEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000800 Genomic DNA. Translation: ABV19758.1. |
| RefSeq | YP_001463045.1. NC_009801.1. |
3D structure databases | |
| ProteinModelPortal | A7ZML6. |
| SMR | A7ZML6. Positions 15-396. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7ZML6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000022027; EBESCP00000021089; EBESCG00000021081. |
| GeneID | 5588995. |
| GenomeReviews | Gene locus EcE24377A_1970 in contig CP000800_GR. |
| KEGG | ecw:EcE24377A_1970. |
| PATRIC | 18293186. VBIEscCol31211_2246. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG4992. |
| GeneTree | EBGT00050000010246. |
| HOGENOM | HBG725944. |
| OMA | PERFRIV. |
| ProtClustDB | PRK12381. |
Enzyme and pathway databases | |
| BioCyc | ECOL331111:ECE24377A_1970-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01173. AstC_aminotrans_3. [Tree] |
| InterPro | IPR017652. Ac/SuccinylOrn_transaminase. 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 | K00840. |
| 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 | 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 | ASTC_ECO24 | ||||||||
| Accession | Primary (citable) accession number: A7ZML6 | ||||||||
| 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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