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Q5R557 (HEM0_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, 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

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 – 4949Mitochondrion By similarity
Chain50 – 5875385-aminolevulinate synthase, erythroid-specific, mitochondrial
PRO_0000290199

Sites

Active site3911 By similarity
Binding site1631Substrate By similarity
Binding site2801Substrate By similarity
Binding site2991Substrate By similarity
Binding site3321Pyridoxal phosphate By similarity
Binding site3601Pyridoxal phosphate By similarity
Binding site3881Pyridoxal phosphate By similarity
Binding site4201Pyridoxal phosphate By similarity
Binding site4211Pyridoxal phosphate By similarity
Binding site5081Substrate By similarity

Amino acid modifications

Modified residue3911N6-(pyridoxal phosphate)lysine

Sequences

Sequence LengthMass (Da)Tools
Q5R557 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: A4DF78C6271D0451

FASTA58764,648
        10         20         30         40         50         60 
MVTAAMLLQC CPVPARGPTS LLGKVVKTHQ FLFGIGRCPI LATQGPNCSQ IHLKATKAGG 

        70         80         90        100        110        120 
DSPSWAKGHC PFMLSELQDG KSKIVQKAAP EVQEDVKAFK TDLPSSLVSA SLKKPFSSPQ 

       130        140        150        160        170        180 
EQEQISGKVT HLIQDNMPGN YVFSYDQFFR DKIMEKKQDH TYRVFKTVNR WADAYPFAQH 

       190        200        210        220        230        240 
FSEASVASKD VSVWCSNDYL GMSRHPQVLR ATQETLQRHG AGAGGTRNIS GTSKFHVELE 

       250        260        270        280        290        300 
QELAELHQKD SALLFSSCFV ANDSTLFTLA KILPGCEIYS DAGNHASMIQ GIRNSGAAKF 

       310        320        330        340        350        360 
VFRHNDPDHL KKLLEKSNPK IPKIVAFEAV HSMDGAICPL EELCDVSHQY GALTFVDEVH 

       370        380        390        400        410        420 
AVGLYGSRGA GIGERDGIMH KIDIISGTLG KAFGCVGGYI ASTRDLVDMV RSYAAGFIFT 

       430        440        450        460        470        480 
TSLPPMVLSG ALESVRLLKG EEGQALRRAH QRNVKHMRQL LMDRGLPVIP CPSHIIPIRV 

       490        500        510        520        530        540 
GNAALNSKLC DLLLSKHGIY VQAINYPTVP RGEELLRLAP SPHHSPQMME DFVEKLLLAW 

       550        560        570        580 
TEVGLPLQDV SVAACNFCRR PVHFELMSEW ERSYFGNMGP QYVTTYA 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR861013 mRNA. Translation: CAH93109.1.
RefSeqNP_001127630.1. NM_001134158.1.
UniGenePab.3363.

3D structure databases

ProteinModelPortalQ5R557.
SMRQ5R557. Positions 1-49.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174709.
KEGGpon:100174709.

Organism-specific databases

CTD212.

Phylogenomic databases

HOVERGENHBG005954.
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. 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_PONAB
AccessionPrimary (citable) accession number: Q5R557
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
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