P49604 (GABAT_USTMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 79.
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: 4-aminobutyrate aminotransferase EC=2.6.1.19 Alternative name(s): GABA aminotransferase Short name=GABA-AT Gamma-amino-N-butyrate transaminase Short name=GABA transaminase | ||||
| Gene names |
| ||||
| Organism | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome] | ||||
| Taxonomic identifier | 237631 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago › ![]() |
Protein attributes
| Sequence length | 509 AA. |
| Sequence status | Complete. |
| 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. Ref.1 |
| 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | gamma-aminobutyric acid catabolic process Inferred from electronic annotation. Source: EnsemblFungi |
| 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521 / FGSC 9021. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U28655 Genomic DNA. Translation: AAA98560.1. AACP01000037 Genomic DNA. Translation: EAK82039.1. |
| PIR | S68116. |
| RefSeq | XP_757227.1. XM_752134.1. |
3D structure databases | |
| ProteinModelPortal | P49604. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 5270.UM01080.1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | UM01080T0; UM01080P0; UM01080. |
| GeneID | 3629154. |
| KEGG | uma:UM01080.1. |
Phylogenomic databases | |
| eggNOG | COG0160. |
| HOGENOM | HOG000020208. |
| KO | K13524. |
| OMA | RLACSFQ. |
| OrthoDB | EOG4HX88H. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 2 hits. |
| InterPro | IPR004631. 4NH2But_aminotransferase_euk. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| PANTHER | PTHR11986. PTHR11986. 1 hit. PTHR11986:SF6. PTHR11986:SF6. 1 hit. |
| Pfam | PF00202. Aminotran_3. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| TIGRFAMs | TIGR00699. GABAtrns_euk. 1 hit. |
| PROSITE | PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GABAT_USTMA | ||||||||
| Accession | Primary (citable) accession number: P49604 Secondary accession number(s): Q4PFN3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
