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Q9XS79 (HEM1_DELLE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 78. 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, 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
Name:ALAS1
Synonyms:ALS1
OrganismDelphinapterus leucas (Beluga whale)
Taxonomic identifier9749 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaCetaceaOdontocetiMonodontidaeDelphinapterus

Protein attributes

Sequence length640 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 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.

Ontologies

Keywords
   Biological processHeme biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function5-aminolevulinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Mitochondrion By similarity
Chain57 – 6405845-aminolevulinate synthase, nonspecific, mitochondrial
PRO_0000001229

Sites

Active site4451 By similarity
Binding site2171Substrate By similarity
Binding site3341Substrate By similarity
Binding site3531Substrate By similarity
Binding site3861Pyridoxal phosphate By similarity
Binding site4141Pyridoxal phosphate By similarity
Binding site4421Pyridoxal phosphate By similarity
Binding site4741Pyridoxal phosphate By similarity
Binding site4751Pyridoxal phosphate By similarity
Binding site5621Substrate By similarity

Amino acid modifications

Modified residue4451N6-(pyridoxal phosphate)lysine Probable

Sequences

Sequence LengthMass (Da)Tools
Q9XS79 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 357BC41CE8EDBA91

FASTA64070,620
        10         20         30         40         50         60 
METVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRALSA SAVLCQQVKE 

        70         80         90        100        110        120 
TPPANEKDKT AKAKVQQAPD GSQQTPDGTQ LPSGHPSLAA SQGTASKCPF LAAQMSQGGS 

       130        140        150        160        170        180 
SVFCKASLEL QEDVQEMHAV REEVAQTSVN PSVISVKTDG GELSGLLKNF QDIMRKQRPE 

       190        200        210        220        230        240 
GVSHLLQDNL PKSVSTFQYD HFFEKKIDEK KNDHTYRVFK TVNRRAQFFP MADDYSDSLV 

       250        260        270        280        290        300 
TKKQVSVWCS NDYLGMSCHP RVCGAVMDTL KQHGTGAGGT RNISGTSKFH VDLEQELADL 

       310        320        330        340        350        360 
HGKDAALLFS SCFVANDSTL FTLAKMMPGC EIYSDSGNHA SMIQGIWNSR VPKYIYRHND 

       370        380        390        400        410        420 
VDHLRELLQR SDPAVPKIVA FETVHSMDGA VCPLEELCDV AHEFGAITFV DEVHAVGLYG 

       430        440        450        460        470        480 
AQGGGIGDRD GVMPKMDIIS GTLGKAFGCV GGYIASTSSL IDTIRSYAAG FIFTTSLPPM 

       490        500        510        520        530        540 
LLAGALESVR ILKSTEGRVL RRQHQRNVKL MRQMLMDASL PVVHCPSHII PVRVADAAKN 

       550        560        570        580        590        600 
TEVCNELMSR HNIYVQAINY PTVRRGEELL RIAPTPHHTP QMMNYFVENL LATWKRVGLE 

       610        620        630        640 
LKPHSSAECN FCRRPLHFEV MSEREKSYFF GMSKLVSAQD 

« 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].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF073337 mRNA. Translation: AAD20806.1.

3D structure databases

ProteinModelPortalQ9XS79.
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. 2 hits.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_DELLE
AccessionPrimary (citable) accession number: Q9XS79
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: October 16, 2013
This is version 78 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