Reviewed,
UniProtKB/Swiss-Prot P38092 (HEM1_EMENI)
Last modified
September 22, 2009.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 5-aminolevulinate synthase, mitochondrial EC=2.3.1.37 Alternative name(s): 5-aminolevulinic acid synthase Delta-aminolevulinate synthase Delta-ALA synthetase | ||||
| Gene names |
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| Organism | Emericella nidulans (Aspergillus nidulans) [Complete proteome] | ||||
| Taxonomic identifier | 162425 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella |
Protein attributes
| Sequence length | 648 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. |
| Pathway | Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. |
| Subcellular location | |
| 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 |
| Gene Ontology (GO) | |
| Biological process | heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| 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 transferase activity, transferring nitrogenous groupsInferred 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 | |||||||
| Chain | ? – 648 | 5-aminolevulinate synthase, mitochondrial | PRO_0000001240 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 412 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 300 | 1 | A → R in CAA45508. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and nucleotide sequence of the 5-aminolevulinate synthase gene from Aspergillus nidulans." Bradshaw R.E., Dixon S.W.C., Raitt D.C., Pillar T.M. Curr. Genet. 23:501-507(1993) [PubMed: 8319309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R153. |
| [2] | "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. Birren B.W.Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4. |
Cross-references
Sequence databases | |
|---|---|
| X64170 Genomic DNA. Translation: CAA45508.1. AACD01000038 Genomic DNA. Translation: EAA64395.1. | |
| PIR | S31846. |
| RefSeq | XP_659888.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FC4 based on UniProtKB P07912. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2874789. |
| KEGG | ani:AN2284.2. |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.37. 3859. |
Family and domain databases | |
| InterPro | IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. 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] |
| TIGRFAMs | TIGR01821. 5aminolev_synth. 1 hit. |
| PROSITE | PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HEM1_EMENI | ||||||||
| Accession | Primary (citable) accession number: P38092 Secondary accession number(s): Q5BAZ6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


