Reviewed,
UniProtKB/Swiss-Prot P53001 (AAT1_BACSU)
Last modified
February 9, 2010.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 393 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. |
| Cofactor | Pyridoxal phosphate. |
| 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 |
| Technical term | Complete proteome |
| 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 – 393 | 393 | Aspartate aminotransferase | PRO_0000123836 | |||||
Sites | |||||||||
| Binding site | 38 | 1 | Aspartate; via amide nitrogen By similarity | ||||||
| Binding site | 124 | 1 | Aspartate By similarity | ||||||
| Binding site | 174 | 1 | Aspartate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 237 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome." Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P. Microbiology 142:2005-2016(1996) [PubMed: 8760912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NCIB 3610. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L47709 Genomic DNA. Translation: AAB38454.1. AL009126 Genomic DNA. Translation: CAB14153.1. |
| PIR | C69591. |
| RefSeq | NP_390118.1. |
3D structure databases | |
| SMR | P53001. Positions 1-391. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 939037. |
| GenomeReviews | Gene locus BSU22370 in contig AL009126_GR. |
| KEGG | bsu:BSU22370. |
| NMPDR | fig|224308.1.peg.2241. |
Organism-specific databases | |
| SubtiList | BG11513. aspB. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG645860. |
| OMA | AYKRTIV. |
| PhylomeDB | P53001. |
Enzyme and pathway databases | |
| BRENDA | 2.6.1.1. 150. |
Family and domain databases | |
| InterPro | IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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 | AAT1_BACSU | ||||||||
| Accession | Primary (citable) accession number: P53001 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with


