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P18080 (HEM0_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-aminolevulinate synthase, erythroid-specific, mitochondrial

Short name=ALAS-E
EC=2.3.1.37
Alternative name(s):
5-aminolevulinic acid synthase 2
Delta-ALA synthase 2
Delta-aminolevulinate synthase 2
Gene names
Name:ALAS2
Synonyms:ALASE
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.

Cofactor

Pyridoxal phosphate.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix.

Tissue specificity

Erythroid specific.

Miscellaneous

There are two delta-ALA synthases 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1818Mitochondrion Potential
Chain19 – 5134955-aminolevulinate synthase, erythroid-specific, mitochondrial
PRO_0000001226

Sites

Active site3231 By similarity
Binding site981Substrate By similarity
Binding site2121Substrate By similarity
Binding site2311Substrate By similarity
Binding site2641Pyridoxal phosphate By similarity
Binding site2921Pyridoxal phosphate By similarity
Binding site3201Pyridoxal phosphate By similarity
Binding site3521Pyridoxal phosphate By similarity
Binding site3531Pyridoxal phosphate By similarity
Binding site4371Substrate By similarity

Amino acid modifications

Modified residue3231N6-(pyridoxal phosphate)lysine Probable

Sequences

Sequence LengthMass (Da)Tools
P18080 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: C319A4DE5294CF74

FASTA51354,778
        10         20         30         40         50         60 
MAAFLRCPLL ARHPPLARAF ATGARCPFMG FAHRAAPELQ EDVERPQIPA VEVLEELLRD 

        70         80         90        100        110        120 
GGAALNRTVR DCMDEDAFPY EEQFQAQLGA LRRTHTYRVV TAVGRRADAP PLGTRGTAPH 

       130        140        150        160        170        180 
TSVELWCSSD YLGLSRHPAV LRAARAALDA HGLGAGGTRN IGGTSPLHGA LERALALLHR 

       190        200        210        220        230        240 
QPRAALFSSC FAANDTALDT LARILPGCQV YSDAGNHASM IQGIRRRGVP KFIFRHNDPH 

       250        260        270        280        290        300 
HLEQLLGRSP PGVPKIVAFE SLHSMDGSIA PLEELCDVAH AYGALTFVDE VHAVGLYGAR 

       310        320        330        340        350        360 
GAGIAERDGV QHKVDVVSGT LGKALGAVGG YIAGSEALVD AVRSLGPGFI FTTALPPQRG 

       370        380        390        400        410        420 
GGALAALQVV GSAEGAALRR AHQRHAKHLR VLLRDRGLPA LPSHIVPVRW DAEANTRLSR 

       430        440        450        460        470        480 
ALLEEHGLYV QAINHPTVPR GQELLLRIAP TPHHSPPMLE NLADKLSECW GAVGLPREDP 

       490        500        510 
PGPSCSSCHR PLHLSLLSPL ERDQFGVRGA AAG 

« Hide

References

[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Erythroid cell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24367 mRNA. Translation: AAA20400.1.
PIRSYCHLE. A31452.

3D structure databases

ProteinModelPortalP18080.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005954.
PhylomeDBP18080.

Enzyme and pathway databases

ReactomeREACT_115655. Metabolism.
UniPathwayUPA00251; UER00375.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010961. 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]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM0_CHICK
AccessionPrimary (citable) accession number: P18080
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways