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Q5R9R9 (HEM1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 59. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

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 By similarity.

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
   Technical termComplete proteome
Reference proteome
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
Chain57 – 6405845-aminolevulinate synthase, nonspecific, mitochondrial
PRO_0000352677

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 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R9R9 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: D0F107895D03F7DA

FASTA64070,514
        10         20         30         40         50         60 
METVVRSCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRALST AAVHYQQIKE 

        70         80         90        100        110        120 
TPPASEKDKT AKAKVQQTPD GSQQSPDGTQ LPSGHPLPAT SQGTASKCPF LAAQMNQRGS 

       130        140        150        160        170        180 
SVFCKASLEL QEDVQEMNAV RKEVAETSGG PSVVSVKTDG GDPSGLLKNF QDIMQKQRPE 

       190        200        210        220        230        240 
RVSHLLQDDL PKSVSTFQYD RFFEKKIDEK KNDHTYRVFK TVNRRAHIFP MADDYSDSLI 

       250        260        270        280        290        300 
TKKQVSVWCS NDYLGMSRHP RVCGAVMDTL KQHGAGAGGT RNISGTSKFH VDLERELADL 

       310        320        330        340        350        360 
HGKDAALLFS SCFVANDSTL FTLAKMMPGC EIYSDSGNHA SMIQGIRNSR VPKYIFRHND 

       370        380        390        400        410        420 
VSHLRELLQR SDPSVPKIVA FETVHSMDGA VCPLEELCDV AHEFGAITFV DEVHAVGLYG 

       430        440        450        460        470        480 
ARGGGIGDRD GVMPKMDIIS GTLGKAFGCV GGYIASTSSL IDTVRSYAAG FIFTTSLPPM 

       490        500        510        520        530        540 
LLAGALESVR ILKSAEGRVL RRQHQRNVKL MRQMLMDAGL PVVHCPSHII PVRVADAAKN 

       550        560        570        580        590        600 
TEVCDELMSR HNIYVQAINY PTVPRGEELL RIAPTPHHTP QMMNYFLENL LVTWKQVGLE 

       610        620        630        640 
LEPHSSAECN FCRRPLHFEV MSEREKSYFS GLSKLVSAQA 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859313 mRNA. Translation: CAH91491.1.
RefSeqNP_001125877.1. NM_001132405.1.

3D structure databases

ProteinModelPortalQ5R9R9.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R9R9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172808.
KEGGpon:100172808.

Organism-specific databases

CTD211.

Phylogenomic databases

HOGENOMHOG000221020.
HOVERGENHBG005954.
InParanoidQ5R9R9.
KOK00643.

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_PONAB
AccessionPrimary (citable) accession number: Q5R9R9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: December 21, 2004
Last modified: October 16, 2013
This is version 59 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