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Q63147 (HEM0_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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:Alase
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Pathway

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

Subunit structure

Interacts with SUCLA2 By similarity. Homodimer.

Subcellular location

Mitochondrion matrix.

Tissue specificity

Erythroid specific.

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_processerythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

female pregnancy

Inferred from expression pattern PubMed 18255020. Source: RGD

heme biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

hemoglobin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

lactation

Inferred from expression pattern PubMed 18255020. Source: RGD

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to drug

Inferred from expression pattern PubMed 16005536. Source: RGD

response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

response to lead ion

Inferred from expression pattern PubMed 16597373. Source: RGD

   Cellular_componentmitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function5-aminolevulinate synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

coenzyme binding

Inferred from direct assay Ref.1. Source: RGD

glycine binding

Inferred from direct assay Ref.1. Source: RGD

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 – ?4949Mitochondrion Potential
Chain?50 – 5875385-aminolevulinate synthase, erythroid-specific, mitochondrial
PRO_0000001225

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 Probable

Sequences

Sequence LengthMass (Da)Tools
Q63147 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A6287CA9543DECAF

FASTA58764,842
        10         20         30         40         50         60 
MVAAAMLLRS CPVLSKGPTG LLGKVAKTYQ FLFGIGRCPI LATQGPTCSQ IHLKATKAGA 

        70         80         90        100        110        120 
DSPSWTKSHC PFMLSELQDR KSKIVQRAAP EVQEDVKTFK TDLLSFMEST TRSQSVPRFQ 

       130        140        150        160        170        180 
DPEQTGGAPP LLIQNNMTGS QAFGYDQFFR DKIMEKKQDH TYRVFKTVNR WANAYPFAQH 

       190        200        210        220        230        240 
FSEASMDSKD VSVWCSNDYL GISRHPRVLQ AIEETLKNHG AGAGGTRNIS GTSKFHVELE 

       250        260        270        280        290        300 
QELAELHHKD SALLFSSCFV ANDSTLFTLA KLLPGCEIYS DAGNHASMIQ GIRNSGAVKF 

       310        320        330        340        350        360 
VFRHNDPGHL KKLLEKSDPK TPKIVAFETV HSMDGAICPL EELCDVAHQY GALTFVDEVH 

       370        380        390        400        410        420 
AVGLYGTRGA GIGERDGIMH KLDIISGTLG KAFGCVGGYI ASTRDLVDMV RSYAAGFIFT 

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

       490        500        510        520        530        540 
GNAALNSKIC DLLLAKHSIY VQAINYPTVP RGEELLRLAP SPHHSPQMME NFVEKLLLAW 

       550        560        570        580 
TEVGLPLQDV SVAACNFCRR PVHFELMSEW ERSYFGNMGP QYVTTYA 

« Hide

References

[1]"Purification and structure of rat erythroid-specific delta-aminolevulinate synthase."
Munakata H., Yamagami T., Nagai T., Yamamoto M., Hayashi N.
J. Biochem. 114:103-111(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]Furuyama K.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86297 mRNA. Translation: BAA13063.1.
PIRJX0278.
RefSeqNP_037329.1. NM_013197.1.
UniGeneRn.226279.
Rn.32517.

3D structure databases

ProteinModelPortalQ63147.
SMRQ63147. Positions 1-49.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ63147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25748.
KEGGrno:25748.

Organism-specific databases

CTD212.
RGD2084. Alas2.

Phylogenomic databases

HOVERGENHBG005954.
KOK00643.
PhylomeDBQ63147.

Enzyme and pathway databases

UniPathwayUPA00251; UER00375.

Gene expression databases

GenevestigatorQ63147.

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...

Other

NextBio607929.
PROQ63147.

Entry information

Entry nameHEM0_RAT
AccessionPrimary (citable) accession number: Q63147
Secondary accession number(s): Q63895
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 95 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