Q75DX7 (HEM1_ASHGO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 65.
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: 5-aminolevulinate synthase, mitochondrial EC=2.3.1.37 Alternative name(s): 5-aminolevulinic acid synthase Delta-ALA synthase Delta-aminolevulinate synthase | ||||
| Gene names |
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| Organism | Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome] | ||||
| Taxonomic identifier | 284811 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium › ![]() |
Protein attributes
| Sequence length | 556 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Heme biosynthesis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Pyridoxal phosphate |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 5-aminolevulinate synthase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 556 | 5-aminolevulinate synthase, mitochondrial | PRO_0000001236 | ||||||
Sites | |||||||||
| Active site | 345 | 1 | By similarity | ||||||
| Binding site | 105 | 1 | Substrate By similarity | ||||||
| Binding site | 218 | 1 | Substrate By similarity | ||||||
| Binding site | 237 | 1 | Substrate By similarity | ||||||
| Binding site | 270 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 298 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 342 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 374 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 375 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 460 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 345 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016815 Genomic DNA. Translation: AAS50667.1. |
| RefSeq | NP_982843.1. NM_208196.1. |
3D structure databases | |
| ProteinModelPortal | Q75DX7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 33169.AGOS_ABL104C. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | AAS50667; AAS50667; AGOS_ABL104C. |
| GeneID | 4618923. |
| KEGG | ago:AGOS_ABL104C. |
Phylogenomic databases | |
| eggNOG | COG0156. |
| HOGENOM | HOG000221020. |
| KO | K00643. |
| OMA | ALPGCHI. |
| OrthoDB | EOG412QDQ. |
| PhylomeDB | Q75DX7. |
Enzyme and pathway databases | |
| UniPathway | UPA00251; UER00375. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 1 hit. |
| InterPro | IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR001917. Aminotrans_II_pyridoxalP_BS. 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. |
| TIGRFAMs | TIGR01821. 5aminolev_synth. 1 hit. |
| PROSITE | PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HEM1_ASHGO | ||||||||
| Accession | Primary (citable) accession number: Q75DX7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
