P34106 (ALA2_PANMI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 68.
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: Alanine aminotransferase 2 Short name=ALAAT-2 EC=2.6.1.2 Alternative name(s): Glutamate pyruvate transaminase 2 Short name=GPT Glutamic--alanine transaminase 2 Glutamic--pyruvic transaminase 2 |
| Organism | Panicum miliaceum (Proso millet) (Broomcorn millet) |
| Taxonomic identifier | 4540 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Paniceae › Panicum![]() |
Protein attributes
| Sequence length | 482 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Transfer of C3 units between the cytosol of mesophyll and bundle sheath cells to maintain a nitrogen-carbon balance in the C4-dicarboxylic pathway. |
| Catalytic activity | L-alanine + 2-oxoglutarate = pyruvate + L-glutamate. |
| Cofactor | Pyridoxal phosphate. |
| Pathway | |
| Subunit structure | Homodimer By similarity. |
| Tissue specificity | Mesophyll and bundle sheath cells. |
| Induction | By light. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase Transferase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | L-alanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway biosynthetic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | L-alanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Molecular cloning of an alanine aminotransferase from NAD-malic enzyme type C4 plant Panicum miliaceum." Son D., Sugiyama T. Plant Mol. Biol. 20:705-713(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 197-206 AND 308-317. Tissue: Leaf. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X69421 mRNA. Translation: CAA49199.1. |
| PIR | S28429. |
3D structure databases | |
| ProteinModelPortal | P34106. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| KEGG | dosa:Os07t0617800-01. dosa:Os10t0390600-01. |
Organism-specific databases | |
| Gramene | P34106. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-17674. |
| UniPathway | UPA00322. UPA00528; UER00586. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 1 hit. |
| InterPro | IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ALA2_PANMI | ||||||||
| Accession | Primary (citable) accession number: P34106 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
