Reviewed,
UniProtKB/Swiss-Prot O33822 (AAT_THEAQ)
Last modified
September 22, 2009.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Aspartate aminotransferase Short name=AspAT EC=2.6.1.1 Alternative name(s): Transaminase A | ||
| Gene names |
| ||
| Organism | Thermus aquaticus | ||
| Taxonomic identifier | 271 [NCBI] | ||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 383 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase Transferase |
| Gene Ontology (GO) | |
| Biological process | biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro L-aspartate:2-oxoglutarate aminotransferase activityInferred 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 – 383 | 383 | Aspartate aminotransferase | PRO_0000123855 | |||||
Amino acid modifications | |||||||||
| Modified residue | 234 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 18 | 1 | A → V in AAB81842. Ref.2 | ||||||
| Sequence conflict | 47 | 1 | E → H in AAB81842. Ref.2 | ||||||
| Sequence conflict | 52 – 53 | 2 | AG → RA in AAB81842. Ref.2 | ||||||
| Sequence conflict | 56 | 1 | A → G in AAB81842. Ref.2 | ||||||
| Sequence conflict | 83 | 1 | R → G in AAB81842. Ref.2 | ||||||
| Sequence conflict | 186 – 187 | 2 | LR → CE in AAB81842. Ref.2 | ||||||
| Sequence conflict | 219 – 220 | 2 | GT → RH in AAB81842. Ref.2 | ||||||
| Sequence conflict | 230 – 231 | 2 | NG → ER in AAB81842. Ref.2 | ||||||
| Sequence conflict | 234 | 1 | K → N in AAB81842. Ref.2 | ||||||
| Sequence conflict | 353 | 1 | E → D in AAB81842. Ref.2 | ||||||
Sequences
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References
| [1] | "Cloning and sequencing of aspartate aminotransferase from Thermus aquaticus YT1." O'Farrell P., Sannia G., Walker J.M., Doonan S. Biochem. Biophys. Res. Commun. 239:810-815(1997) [PubMed: 9367851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: YT1. |
| [2] | Benner E., Ramaley R.F. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: YT1. |
Cross-references
Sequence databases | |
|---|---|
| X99521 Genomic DNA. Translation: CAA67877.1. AF025665 Genomic DNA. Translation: AAB81842.1. | |
| PIR | JC5775. |
3D structure databases | |
| SMR | O33822. Positions 1-382. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.6.1.1. 118. |
Family and domain databases | |
| InterPro | IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| PRINTS | PR00753. ACCSYNTHASE. |
| PROSITE | PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AAT_THEAQ | ||||||||
| Accession | Primary (citable) accession number: O33822 Secondary accession number(s): O31028 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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