A6QLI6 (HEM1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 46.
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, nonspecific, mitochondrial Short name=ALAS-H EC=2.3.1.37 Alternative name(s): 5-aminolevulinic acid synthase 1 Delta-ALA synthase 1 Delta-aminolevulinate synthase 1 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 647 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
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. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Miscellaneous | There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues 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 nucleusInferred from electronic annotation. Source: Compara |
| 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 – 56 | 56 | Mitochondrion By similarity | ||||||
| Chain | 57 – 647 | 591 | 5-aminolevulinate synthase, nonspecific, mitochondrial | PRO_0000352676 | |||||
Sites | |||||||||
| Active site | 452 | 1 | By similarity | ||||||
| Binding site | 224 | 1 | Substrate By similarity | ||||||
| Binding site | 341 | 1 | Substrate By similarity | ||||||
| Binding site | 360 | 1 | Substrate By similarity | ||||||
| Binding site | 393 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 421 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 449 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 481 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 482 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 569 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 452 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Brain cortex. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC147978 mRNA. Translation: AAI47979.1. |
| IPI | IPI00706740. |
| RefSeq | NP_001094624.1. NM_001101154.1. |
| UniGene | Bt.15857. |
3D structure databases | |
| ProteinModelPortal | A6QLI6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000005380. |
Proteomic databases | |
| PRIDE | A6QLI6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000005380; ENSBTAP00000005380; ENSBTAG00000004118. |
| GeneID | 534286. |
| KEGG | bta:534286. |
Organism-specific databases | |
| CTD | 211. |
Phylogenomic databases | |
| eggNOG | COG0156. |
| GeneTree | ENSGT00530000063111. |
| HOGENOM | HOG000221020. |
| HOVERGEN | HBG005954. |
| InParanoid | A6QLI6. |
| KO | K00643. |
| OMA | ALPGCHI. |
| OrthoDB | EOG42V8FW. |
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. IPR015118. 5aminolev_synth_preseq. 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. PF09029. Preseq_ALAS. 2 hits. [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... |
Other | |
| NextBio | 20876339. |
Entry information
| Entry name | HEM1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: A6QLI6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
