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Q9YHT4 (HEM0_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:alas-e
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length583 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 metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix.

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 caution

The sequence AAH67149.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 5835-aminolevulinate synthase, erythroid-specific, mitochondrialPRO_0000001227

Sites

Active site3861 By similarity
Binding site1581Substrate By similarity
Binding site2751Substrate By similarity
Binding site3271Pyridoxal phosphate By similarity
Binding site3551Pyridoxal phosphate By similarity
Binding site3831Pyridoxal phosphate By similarity
Binding site4151Pyridoxal phosphate By similarity
Binding site4161Pyridoxal phosphate By similarity
Binding site5031Substrate By similarity

Amino acid modifications

Modified residue3861N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YHT4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 9C542B4C75299ABD

FASTA58363,909
        10         20         30         40         50         60 
MSAFLHHCPF LKSSPGPSAR KVATYLNLAD RCPIIVRQIS AKAAQSSEQN GLLPHKEPKR 

        70         80         90        100        110        120 
QLATTATQVA VSMSQSCPFV SSKIGLVKAS PQVQEDVQPN LENQDTSGLI SSLFSGLQSH 

       130        140        150        160        170        180 
QSTGPTHLLQ DNFNRPTFSY DEFFTQKIVE KKKDHTYRIF KTVNRFAEVF PFAEDYSIAG 

       190        200        210        220        230        240 
RLGSQVSVWC SNDYLGMSRH PRVVKAIGDA LKKHGAGAGG TRNISGTSNY HVALENELAR 

       250        260        270        280        290        300 
LHQKDGALVF SSCFVANDST LFTLAKMLPG CEIYSDMGNH ASMIQGIRNS GAKRFIFRHN 

       310        320        330        340        350        360 
DASHLEELLS RSDPLTPKIV AFETVHSMDG AICPLEELCD VAHKYGALTF VDEVHAVGLY 

       370        380        390        400        410        420 
GAHGAGVGER DNVMHKIDIV SGTLGKAFGC VGGYIASTAA LVDTVRSFAA GFIFTTSLPP 

       430        440        450        460        470        480 
MVLAGALESV RVLKSDEGQA LRRAHQRNVK HMRQLLLDAG LPVVNCPSHI IPIRVGNAAK 

       490        500        510        520        530        540 
NSEVCDILLE KHNIYVQAIN YPTVPRGEEL LRLAPSPFHN PIMMNYFAEK LLDVWQEVGL 

       550        560        570        580 
PLNGPAQASC TFCDRPLHFD LMSEWEKSYF GNMEPRYITV AAQ

« Hide

References

« Hide 'large scale' references
[1]"Positional cloning of the zebrafish sauternes gene: a model for congenital sideroblastic anaemia."
Brownlie A., Donovan A., Pratt S.J., Paw B.H., Oates A.C., Brugnara C., Witkowska H.E., Sassa S., Zon L.I.
Nat. Genet. 20:244-250(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF095747 mRNA. Translation: AAC72835.1.
BC056338 mRNA. Translation: AAH56338.1.
BC067149 mRNA. Translation: AAH67149.1. Different initiation.
IPIIPI00490337.
RefSeqNP_571757.1. NM_131682.2.
UniGeneDr.8180.

3D structure databases

ProteinModelPortalQ9YHT4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000056420; ENSDARP00000056419; ENSDARG00000038643.
GeneID64607.
KEGGdre:64607.

Organism-specific databases

CTD212.
ZFINZDB-GENE-001229-1. alas2.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00530000063111.
HOGENOMHOG000221020.
HOVERGENHBG005954.
InParanoidQ9YHT4.
KOK00643.
OrthoDBEOG4H19VB.

Enzyme and pathway databases

UniPathwayUPA00251; UER00375.

Gene expression databases

ArrayExpressQ9YHT4.
BgeeQ9YHT4.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010961. 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]
PfamPF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20901975.

Entry information

Entry nameHEM0_DANRE
AccessionPrimary (citable) accession number: Q9YHT4
Secondary accession number(s): Q6NXC5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 1999
Last modified: April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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