Reviewed,
UniProtKB/Swiss-Prot P07997 (HEM1_CHICK)
Last modified
June 16, 2009.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: 5-aminolevulinate synthase, nonspecific, mitochondrial EC=2.3.1.37 Alternative name(s): 5-aminolevulinic acid synthase Delta-aminolevulinate synthase Delta-ALA synthetase Short name=ALAS-H | ||||
| Gene names |
| ||||
| Organism | Gallus gallus (Chicken) | ||||
| Taxonomic identifier | 9031 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus |
Protein attributes
| Sequence length | 635 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. |
| Pathway | Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Miscellaneous | There are two delta-ALA synthetase in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues. |
| 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 |
| 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 – 56 | 56 | Mitochondrion | ||||||
| Chain | 57 – 635 | 579 | 5-aminolevulinate synthase, nonspecific, mitochondrial | PRO_0000001233 | |||||
Amino acid modifications | |||||||||
| Modified residue | 440 | 1 | N6-(pyridoxal phosphate)lysine Probable | ||||||
Experimental info | |||||||||
| Sequence conflict | 53 | 1 | S → A Ref.2 | ||||||
| Sequence conflict | 53 | 1 | S → A Ref.3 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Nucleotide sequence of the chicken 5-aminolevulinate synthase gene." Maguire D.J., Day A.R., Borthwick I.A., Srivastava G., Wigley P.L., May B.K., Elliott W.H. Nucleic Acids Res. 14:1379-1391(1986) [PubMed: 3005973] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver. |
| [2] | "Complete nucleotide sequence of hepatic 5-aminolaevulinate synthase precursor." Borthwick I.A., Srivastava G., Day A.R., Pirola B.A., Snoswell M.A., May B.K., Elliott W.H. Eur. J. Biochem. 150:481-484(1985) [PubMed: 3839458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [3] | "Expression of delta-aminolevulinate synthase in avian cells: separate genes encode erythroid-specific and nonspecific isozymes." Riddle R.D., Yamamoto M., Engel J.D. Proc. Natl. Acad. Sci. U.S.A. 86:792-796(1989) [PubMed: 2915978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| X02827 mRNA. Translation: CAA26595.1. X03517, X03627 Genomic DNA. Translation: CAA27223.1. | |
| IPI | IPI00584086. |
| PIR | SYCHAL. A23538. |
| RefSeq | NP_001018012.1. |
| UniGene | Gga.1399 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BS0 based on UniProtKB P12998. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 552895. |
| KEGG | gga:552895. |
Phylogenomic databases | |
| HOVERGEN | P07997. |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.37. 4. |
Family and domain databases | |
| InterPro | IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR004839. Aminotrans_I/II. IPR001917. Aminotrans_II_pyridoxalP_BS. 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_CHICK | ||||||||
| Accession | Primary (citable) accession number: P07997 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


