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Protein

5-aminolevulinate synthase

Gene

Alas2

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: MGI
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular iron ion homeostasis Source: MGI
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  3. response to hypoxia Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotation, Transferase

Keywords - Biological processi

Heme biosynthesisUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthaseUniRule annotation (EC:2.3.1.37UniRule annotation)
Alternative name(s):
5-aminolevulinic acid synthaseUniRule annotation
Delta-ALA synthaseUniRule annotation
Delta-aminolevulinate synthaseUniRule annotation
Gene namesi
Name:Alas2Imported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Organism-specific databases

MGIiMGI:87990. Alas2.

Subcellular locationi

Mitochondrion matrix UniRule annotation

GO - Cellular componenti

  1. mitochondrial inner membrane Source: MGI
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

MitochondrionUniRule annotation

PTM / Processingi

Proteomic databases

PRIDEiA2AFM0.

Expressioni

Gene expression databases

ExpressionAtlasiA2AFM0. baseline and differential.
GenevestigatoriA2AFM0.

Structurei

3D structure databases

ProteinModelPortaliA2AFM0.
SMRiA2AFM0. Positions 1-49, 151-540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.UniRule annotation

Phylogenomic databases

HOVERGENiHBG005954.
KOiK00643.
OMAiRAEKYIY.
PhylomeDBiA2AFM0.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 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]
PfamiPF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2AFM0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVAAAMLLRS CPVLSQGPTG LLGKVAKTYQ FLFSIGRCPI LATQGPTCSQ
60 70 80 90 100
IHLKATKAGG DSPSWAKSHC PFMLSELQDR KSKIVQRAAP EVQEDVKTFK
110 120 130 140 150
TDLLSTMDST TRSHSFPSFQ EPEQTEGAVP HLIQNNMTGS QAFGYDQFFR
160 170 180 190 200
DKIMEKKQDH TYRVFKTVNR WANAYPFAQH FSEASMASKD VSVWCSNDYL
210 220 230 240 250
GISRHPRVLQ AIEETLKNHG AGAGGTRNIS GTSKFHVELE QELAELHQKD
260 270 280 290 300
SALLFSSCFV ANDSTLFTLA KLLPGCEIYS DAGNHASMIQ GIRNSGAAKF
310 320 330 340 350
VFRHNDPGHL KKLLEKSDPK TPKIVAFETV HSMDGAICPL EELCDVAHQY
360 370 380 390 400
GALTFVDEVH AVGLYGARGA GIGERDGIMH KLDIISGTLG KAFGCVGGYI
410 420 430 440 450
ASTRDLVDMV RSYAAGFIFT TSLPPMVLSG ALESVRLLKG EEGQALRRAH
460 470 480 490 500
QRNVKHMRQL LMDRGFPVIP CPSHIIPIRV GNAALNSKIC DLLLSKHSIY
510 520 530 540 550
VQAINYPTVP RGEELLRLAP SPHHSPQMME NFVEKLLLAW TEVGLPLQDV
560 570 580
SVAACNFCHR PVHFELMSEW ERSYFGNMGP QYVTTYA
Length:587
Mass (Da):64,753
Last modified:February 20, 2007 - v1
Checksum:iA878D79FAD5B9856
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC150870 mRNA. Translation: AAI50871.1.
RefSeqiNP_033783.1. NM_009653.3.
UniGeneiMm.302724.

Genome annotation databases

GeneIDi11656.
KEGGimmu:11656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC150870 mRNA. Translation: AAI50871.1.
RefSeqiNP_033783.1. NM_009653.3.
UniGeneiMm.302724.

3D structure databases

ProteinModelPortaliA2AFM0.
SMRiA2AFM0. Positions 1-49, 151-540.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA2AFM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi11656.
KEGGimmu:11656.

Organism-specific databases

CTDi212.
MGIiMGI:87990. Alas2.

Phylogenomic databases

HOVERGENiHBG005954.
KOiK00643.
OMAiRAEKYIY.
PhylomeDBiA2AFM0.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.

Miscellaneous databases

NextBioi279269.
SOURCEiSearch...

Gene expression databases

ExpressionAtlasiA2AFM0. baseline and differential.
GenevestigatoriA2AFM0.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 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]
PfamiPF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported.

Entry informationi

Entry nameiA2AFM0_MOUSE
AccessioniPrimary (citable) accession number: A2AFM0
Entry historyi
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: February 4, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.UniRule annotation

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.