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Protein

5-aminolevulinate synthase, erythroid-specific, mitochondrial

Gene

Alas2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from glycine.
Proteins known to be involved in this subpathway in this organism are:
  1. 5-aminolevulinate synthase (Alas2), 5-aminolevulinate synthase (Alas2), 5-aminolevulinate synthase (Alas2), 5-aminolevulinate synthase (Alas1), 5-aminolevulinate synthase, erythroid-specific, mitochondrial (Alas2), 5-aminolevulinate synthase, nonspecific, mitochondrial (Alas1), 5-aminolevulinate synthase (Alas2), 5-aminolevulinate synthase (Alas2), 5-aminolevulinate synthase (Alas1)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from glycine, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei163SubstrateBy similarity1
Binding sitei280SubstrateBy similarity1
Binding sitei299SubstrateBy similarity1
Binding sitei332Pyridoxal phosphateBy similarity1
Binding sitei360Pyridoxal phosphateBy similarity1
Binding sitei388Pyridoxal phosphateBy similarity1
Active sitei391By similarity1
Binding sitei420Pyridoxal phosphate; shared with dimeric partnerBy similarity1
Binding sitei421Pyridoxal phosphate; shared with dimeric partnerBy similarity1
Binding sitei508SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cellular iron ion homeostasis Source: MGI
  • erythrocyte differentiation Source: UniProtKB
  • heme biosynthetic process Source: UniProtKB
  • hemoglobin biosynthetic process Source: UniProtKB
  • protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  • response to hypoxia Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-MMU-189451. Heme biosynthesis.
UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase, erythroid-specific, mitochondrial (EC:2.3.1.37)
Short name:
ALAS-E
Alternative name(s):
5-aminolevulinic acid synthase 2
Delta-ALA synthase 2
Delta-aminolevulinate synthase 2
Gene namesi
Name:Alas2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:87990. Alas2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi391K → A or H: Abolishes enzyme activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 49Mitochondrion1 PublicationAdd BLAST49
ChainiPRO_000000122450 – 5875-aminolevulinate synthase, erythroid-specific, mitochondrialAdd BLAST538

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei391N6-(pyridoxal phosphate)lysine1 Publication1

Proteomic databases

PaxDbiP08680.
PRIDEiP08680.

PTM databases

PhosphoSitePlusiP08680.

Expressioni

Tissue specificityi

Erythroid specific.

Gene expression databases

BgeeiENSMUSG00000025270.
CleanExiMM_ALAS2.
ExpressionAtlasiP08680. baseline and differential.
GenevisibleiP08680. MM.

Interactioni

Subunit structurei

Interacts with SUCLA2 (By similarity). Homodimer.By similarity

Protein-protein interaction databases

BioGridi198059. 1 interactor.
IntActiP08680. 4 interactors.
STRINGi10090.ENSMUSP00000066040.

Structurei

Secondary structure

1587
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 8Combined sources4
Beta strandi14 – 16Combined sources3
Turni23 – 27Combined sources5
Helixi28 – 32Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H7DNMR-A1-49[»]
1H7JNMR-A1-26[»]
ProteinModelPortaliP08680.
SMRiP08680.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08680.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1360. Eukaryota.
COG0156. LUCA.
GeneTreeiENSGT00530000063111.
HOGENOMiHOG000221020.
HOVERGENiHBG005954.
InParanoidiP08680.
KOiK00643.
OMAiNFPFAEH.
OrthoDBiEOG091G043U.
PhylomeDBiP08680.
TreeFamiTF300724.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08680-1 [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:January 23, 2002 - v3
Checksum:iA878D79FAD5B9856
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61 – 75Missing in AAA37207 (PubMed:3557128).CuratedAdd BLAST15
Sequence conflicti66A → R in BAB22254 (PubMed:16141072).Curated1
Sequence conflicti171W → R in AAA91866 (Ref. 2) Curated1
Sequence conflicti338C → V in AAA91866 (Ref. 2) Curated1
Sequence conflicti368 – 372RGAGI → GVQVS in AAA91866 (Ref. 2) Curated5
Sequence conflicti427V → M in AAA37207 (PubMed:3557128).Curated1
Sequence conflicti479R → W in AAA91866 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15268 mRNA. Translation: AAA37207.1. Different initiation.
M63244 mRNA. Translation: AAA91866.1.
AK002642 mRNA. Translation: BAB22254.1.
AK077610 mRNA. Translation: BAC36898.1.
CCDSiCCDS41173.1.
PIRiA29040. SYMSAL.
RefSeqiNP_001095916.1. NM_001102446.1.
NP_033783.1. NM_009653.3.
UniGeneiMm.302724.

Genome annotation databases

EnsembliENSMUST00000066337; ENSMUSP00000066040; ENSMUSG00000025270.
GeneIDi11656.
KEGGimmu:11656.
UCSCiuc009uoj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15268 mRNA. Translation: AAA37207.1. Different initiation.
M63244 mRNA. Translation: AAA91866.1.
AK002642 mRNA. Translation: BAB22254.1.
AK077610 mRNA. Translation: BAC36898.1.
CCDSiCCDS41173.1.
PIRiA29040. SYMSAL.
RefSeqiNP_001095916.1. NM_001102446.1.
NP_033783.1. NM_009653.3.
UniGeneiMm.302724.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H7DNMR-A1-49[»]
1H7JNMR-A1-26[»]
ProteinModelPortaliP08680.
SMRiP08680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198059. 1 interactor.
IntActiP08680. 4 interactors.
STRINGi10090.ENSMUSP00000066040.

PTM databases

PhosphoSitePlusiP08680.

Proteomic databases

PaxDbiP08680.
PRIDEiP08680.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066337; ENSMUSP00000066040; ENSMUSG00000025270.
GeneIDi11656.
KEGGimmu:11656.
UCSCiuc009uoj.1. mouse.

Organism-specific databases

CTDi212.
MGIiMGI:87990. Alas2.

Phylogenomic databases

eggNOGiKOG1360. Eukaryota.
COG0156. LUCA.
GeneTreeiENSGT00530000063111.
HOGENOMiHOG000221020.
HOVERGENiHBG005954.
InParanoidiP08680.
KOiK00643.
OMAiNFPFAEH.
OrthoDBiEOG091G043U.
PhylomeDBiP08680.
TreeFamiTF300724.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.
ReactomeiR-MMU-189451. Heme biosynthesis.

Miscellaneous databases

EvolutionaryTraceiP08680.
PROiP08680.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025270.
CleanExiMM_ALAS2.
ExpressionAtlasiP08680. baseline and differential.
GenevisibleiP08680. MM.

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...

Entry informationi

Entry nameiHEM0_MOUSE
AccessioniPrimary (citable) accession number: P08680
Secondary accession number(s): Q64452, Q9DCN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2002
Last modified: November 30, 2016
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.