Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08680 (HEM0_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Sequence caution

The sequence AAA37207.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4949Mitochondrion
Chain50 – 5875385-aminolevulinate synthase, erythroid-specific, mitochondrial
PRO_0000001224

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

Experimental info

Mutagenesis3911K → A or H: Abolishes enzyme activity.
Sequence conflict61 – 7515Missing in AAA37207. Ref.1
Sequence conflict661A → R in BAB22254. Ref.3
Sequence conflict1711W → R in AAA91866. Ref.2
Sequence conflict3381C → V in AAA91866. Ref.2
Sequence conflict368 – 3725RGAGI → GVQVS in AAA91866. Ref.2
Sequence conflict4271V → M in AAA37207. Ref.1
Sequence conflict4791R → W in AAA91866. Ref.2

Secondary structure

........ 587
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08680 [UniParc].

Last modified January 23, 2002. Version 3.
Checksum: A878D79FAD5B9856

FASTA58764,753
        10         20         30         40         50         60 
MVAAAMLLRS CPVLSQGPTG LLGKVAKTYQ FLFSIGRCPI LATQGPTCSQ IHLKATKAGG 

        70         80         90        100        110        120 
DSPSWAKSHC PFMLSELQDR KSKIVQRAAP EVQEDVKTFK TDLLSTMDST TRSHSFPSFQ 

       130        140        150        160        170        180 
EPEQTEGAVP HLIQNNMTGS QAFGYDQFFR DKIMEKKQDH TYRVFKTVNR WANAYPFAQH 

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

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

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

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

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

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

       550        560        570        580 
TEVGLPLQDV SVAACNFCHR PVHFELMSEW ERSYFGNMGP QYVTTYA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of mouse 5-aminolevulinic acid synthase cDNA and expression of its gene in hepatic and erythroid tissues."
Schoenhaut D.S., Curtis P.J.
Gene 48:55-63(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Two genes encode Ala synthase in DBA/2 mouse: housekeeping and erythroid-specific."
Young E.G., Dierks P.M.
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: DBA/2.
Tissue: Erythroleukemia.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[4]"Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5'-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase."
Ferreira G.C., Neame P.J., Dailey H.A.
Protein Sci. 2:1959-1965(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PYRIDOXAL PHOSPHATE AT LYS-391.
[5]"The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase."
Goodfellow B.J., Dias J.S., Ferreira G.C., Henklein P., Wray V., Macedo A.L.
FEBS Lett. 505:325-331(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-49, TRANSIT PEPTIDE CLEAVAGE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15268 mRNA. Translation: AAA37207.1. Different initiation.
M63244 mRNA. Translation: AAA91866.1.
AK002642 mRNA. Translation: BAB22254.1.
AK077610 mRNA. Translation: BAC36898.1.
CCDSCCDS41173.1.
PIRSYMSAL. A29040.
RefSeqNP_001095916.1. NM_001102446.1.
NP_033783.1. NM_009653.3.
UniGeneMm.302724.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H7DNMR-A1-49[»]
1H7JNMR-A1-26[»]
ProteinModelPortalP08680.
SMRP08680. Positions 1-49, 151-540.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198059. 1 interaction.

PTM databases

PhosphoSiteP08680.

Proteomic databases

PaxDbP08680.
PRIDEP08680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066337; ENSMUSP00000066040; ENSMUSG00000025270.
GeneID11656.
KEGGmmu:11656.
UCSCuc009uoj.1. mouse.

Organism-specific databases

CTD212.
MGIMGI:87990. Alas2.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00530000063111.
HOGENOMHOG000221020.
HOVERGENHBG005954.
InParanoidP08680.
KOK00643.
OMAHYLQSIN.
OrthoDBEOG7TQV0F.
PhylomeDBP08680.
TreeFamTF300724.

Enzyme and pathway databases

UniPathwayUPA00251; UER00375.

Gene expression databases

ArrayExpressP08680.
BgeeP08680.
CleanExMM_ALAS2.
GenevestigatorP08680.

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

EvolutionaryTraceP08680.
NextBio279269.
PROP08680.
SOURCESearch...

Entry information

Entry nameHEM0_MOUSE
AccessionPrimary (citable) accession number: P08680
Secondary accession number(s): Q64452, Q9DCN0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 141 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot