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Q9XT75 (HEM0_DELLE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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:ALS2
OrganismDelphinapterus leucas (Beluga whale)
Taxonomic identifier9749 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaCetaceaOdontocetiMonodontidaeDelphinapterus

Protein attributes

Sequence length582 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 By similarity.

Pathway

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

Subunit structure

Homodimer. Interacts with SUCLA2 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.

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 – ?4444Mitochondrion Potential
Chain?45 – 5825385-aminolevulinate synthase, erythroid-specific, mitochondrial
PRO_0000001222

Sites

Active site3861 By similarity
Binding site1581Substrate By similarity
Binding site2751Substrate By similarity
Binding site2941Substrate 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
Q9XT75 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 7C15EBF6C154C34D

FASTA58264,555
        10         20         30         40         50         60 
MLLQRCPVLI RSPTAILGKM IKTHQFLIGI GRCPILATQG TTCSQIHLKA TKAGGDSPSW 

        70         80         90        100        110        120 
AKSHCPFMLL ELQDGKSKIV QKAAPEVQED VKTFKTDLPI SLASTSLRKP FFSPQEPEKN 

       130        140        150        160        170        180 
SEKVTHLIQN NMAGNHVFGY DQFFRNKIME KKQDHTYRVF KTVNRWADAY PFAEHFFEAS 

       190        200        210        220        230        240 
VASKDVSVWC SNDYLGMSRH PRVLQATQET LQRHGAGAGG TRNISGTSRF HVELEQELAE 

       250        260        270        280        290        300 
LHQKDSALLF SSCFVANDST LFTLAKILPG CEIYSDAGNH ASMIQGIRNS GAAKFVFRHN 

       310        320        330        340        350        360 
DPDHLKKLLK KSNPETPKIV AFETVHSMDG AICPLEELCD VAHQYGALTF VDEVHAVGLY 

       370        380        390        400        410        420 
GSRGAGIGER DGIMHKIDII SGTLGKAFGC VGGYIASTRD LVDMVRSYAA GFIFTTSLPP 

       430        440        450        460        470        480 
MVLSGALESV RLLKGEEGQA LRRAHQRNVK HMRQLLMDRG LPVIPCPSHI IPIRVGDAAL 

       490        500        510        520        530        540 
NSRICDLLLS KHGIYVQAIN YPTVPRGEEL LRLAPSPHHS PQMMEDFVEK LLAAWTEVGL 

       550        560        570        580 
PLQDVSIAAC NFCRRPVHFE LMSEWERSYF GNMGPQYVTT YA 

« Hide

References

[1]"Comparison of the beluga whale (Delphinapterus leucas) expressed genes for 5-aminolevulinate synthase with those in other vertebrates."
Kreiling J.A., Duncan R., Faggart M.A., Cornell N.W.
Comp. Biochem. Physiol. 123B:163-174(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF086786 mRNA. Translation: AAD41464.1.

3D structure databases

ProteinModelPortalQ9XT75.
SMRQ9XT75. Positions 1-44.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005954.

Enzyme and pathway databases

UniPathwayUPA00251; UER00375.

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. SSF53383. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM0_DELLE
AccessionPrimary (citable) accession number: Q9XT75
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 79 of the entry and version 1 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