Reviewed,
UniProtKB/Swiss-Prot P49604 (GATA_USTMA)
Last modified
November 3, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 4-aminobutyrate aminotransferase EC=2.6.1.19 Alternative name(s): Gamma-amino-N-butyrate transaminase Short name=GABA transaminase GABA aminotransferase Short name=GABA-AT | ||||
| Gene names |
| ||||
| Organism | Ustilago maydis (Smut fungus) [Complete proteome] | ||||
| Taxonomic identifier | 5270 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago |
Protein attributes
| Sequence length | 509 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Deaminates gamma-aminobutyric acid (GABA) to succinate-semialdehyde, which in turn is converted to succinate by the succinate semialdehyde dehydrogenase By similarity. Not required for the utilization of GABA as nitrogen source. |
| Catalytic activity | 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate. |
| Cofactor | Pyridoxal phosphate. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Induction | Up-regulated by GABA and beta-alanine. Is not subject to nitrogen catabolite repression. Ref.1 |
| Sequence similarities | Belongs to the class-III 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 | gamma-aminobutyric acid metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4-aminobutyrate transaminase activity Inferred 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 – 509 | 509 | 4-aminobutyrate aminotransferase | PRO_0000120381 | |||||
Amino acid modifications | |||||||||
| Modified residue | 363 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 337 | 1 | G → GT in AAA98560. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of the ugatA gene of Ustilago maydis, isolated by homology to the gatA gene of Aspergillus nidulans." Straffon M.J., Hynes M.J., Davis M.A. Curr. Genet. 29:360-369(1996) [PubMed: 8598057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION. Strain: 518. |
| [2] | "Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. Birren B.W.Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521. |
Cross-references
Sequence databases | |
|---|---|
| U28655 Genomic DNA. Translation: AAA98560.1. AACP01000037 Genomic DNA. Translation: EAK82039.1. | |
| PIR | S68116. |
| RefSeq | XP_757227.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GTX based on UniProtKB P80147. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P49604. |
Genome annotation databases | |
| GeneID | 3629154. |
| KEGG | uma:UM01080.1. |
Phylogenomic databases | |
| OMA | KERGQRG. |
Enzyme and pathway databases | |
| BRENDA | 2.6.1.19. 2320. |
Family and domain databases | |
| InterPro | IPR004631. 4NH2But_aminotransferase_euk. IPR005814. Aminotrans_3. [Graphical view] |
| PANTHER | PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF6. GABAtrns_euk. 1 hit. |
| Pfam | PF00202. Aminotran_3. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00699. GABAtrns_euk. 1 hit. |
| PROSITE | PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GATA_USTMA | ||||||||
| Accession | Primary (citable) accession number: P49604 Secondary accession number(s): Q4PFN3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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