ALAS2
entrez
212
canonical
uniprot
P22557
canonical
ensembl
ENSG00000158578
resolver
ensp
ENSP00000337131
resolver
ensp
ENSP00000379501
resolver
ensp
ENSP00000497236
resolver
genesymbol
ALAS2
resolver
genesymbol_syn
ALASE
resolver
genesymbol_syn
ASB
resolver
hgnc
HGNC:397
resolver
uniprot
A8K3F0
resolver
uniprot
A8K6C4
resolver
uniprot
Q13735
resolver
uniprot
Q5JZF5
resolver
uniprot
Q8N6H3
resolver
uniprot_entry
HEM0_HUMAN
resolver
uniprot_sec
A8K3F0
resolver
uniprot_sec
A8K6C4
resolver
uniprot_sec
Q13735
resolver
uniprot_sec
Q5JZF5
resolver
uniprot_sec
Q8N6H3
resolver
activity_regulation
ACTIVITY REGULATION: Down-regulated by itaconyl-CoA which acts as a competitive inhibitor of succinyl-CoA substrate. {ECO:0000269|PubMed:34492704}.
uniprot
proteins
amino_acid_sequence
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGGDSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQEQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
uniprot
proteins
disease_involvement
DISEASE: Anemia, sideroblastic, 1 (SIDBA1) [MIM:300751]: A form of sideroblastic anemia that shows a variable hematologic response to pharmacologic doses of pyridoxine. Sideroblastic anemia is characterized by anemia of varying severity, hypochromic peripheral erythrocytes, systemic iron overload secondary to chronic ineffective erythropoiesis, and the presence of bone marrow ringed sideroblasts. Sideroblasts are characterized by iron-loaded mitochondria clustered around the nucleus. {ECO:0000269|PubMed:10029606, ECO:0000269|PubMed:10577279, ECO:0000269|PubMed:12031592, ECO:0000269|PubMed:12393718, ECO:0000269|PubMed:1570328, ECO:0000269|PubMed:16446107, ECO:0000269|PubMed:19731322, ECO:0000269|PubMed:21252495, ECO:0000269|PubMed:21309041, ECO:0000269|PubMed:8107717, ECO:0000269|PubMed:9858242}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Erythropoietic protoporphyria, X-linked dominant (XLDPT) [MIM:300752]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. XLDPT is characterized biochemically by a high proportion of zinc-protoporphyrin in erythrocytes, in which a mismatch between protoporphyrin production and the heme requirement of differentiating erythroid cells leads to overproduction of protoporphyrin in amounts sufficient to cause photosensitivity and liver disease. {ECO:0000269|PubMed:18760763}. Note=The disease is caused by variants affecting the gene represented in this entry. Gain of function mutations in ALS2 are responsible for XLDPT, but they can also be a possible aggravating factor in congenital erythropoietic porphyria and other erythropoietic disorders caused by mutations in other genes (PubMed:21309041). {ECO:0000269|PubMed:21309041}.
uniprot
proteins
ec_number
2.3.1.37
uniprot
proteins
function
FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed:14643893, PubMed:21252495, PubMed:21309041, PubMed:21653323, PubMed:32499479, PubMed:34492704). Contributes significantly to heme formation during erythropoiesis (PubMed:2050125). {ECO:0000269|PubMed:14643893, ECO:0000269|PubMed:21252495, ECO:0000269|PubMed:21309041, ECO:0000269|PubMed:21653323, ECO:0000269|PubMed:32499479, ECO:0000269|PubMed:34492704, ECO:0000303|PubMed:2050125}.; FUNCTION: [Isoform 3]: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed:14643893). Catalytic activity is 75-85% of isoform 1 activity (PubMed:14643893). {ECO:0000269|PubMed:14643893}.; FUNCTION: [Isoform 4]: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed:14643893). Catalytic activity is 65-75% of isoform 1 activity (PubMed:14643893). {ECO:0000269|PubMed:14643893}.
uniprot
proteins
mass_dalton
64633
uniprot
proteins
mutagenesis
MUTAGEN 511; /note="R->E: 2-fold increased enzyme activity with a lower specificity for glycine and higher for succinyl-CoA."; /evidence="ECO:0000269|PubMed:32499479
uniprot
proteins
pathway_participation
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. {ECO:0000305|PubMed:32499479}.
uniprot
proteins
protein_family
Class-II pyridoxal-phosphate-dependent aminotransferase family
uniprot
proteins
pubmed
10029606
uniprot
proteins
pubmed
10577279
uniprot
proteins
pubmed
12031592
uniprot
proteins
pubmed
12393718
uniprot
proteins
pubmed
14643893
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1570328
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16446107
uniprot
proteins
pubmed
18760763
uniprot
proteins
pubmed
19731322
uniprot
proteins
pubmed
2050125
uniprot
proteins
pubmed
21252495
uniprot
proteins
pubmed
21309041
uniprot
proteins
pubmed
21653323
uniprot
proteins
pubmed
2263504
uniprot
proteins
pubmed
32499479
uniprot
proteins
pubmed
34492704
uniprot
proteins
pubmed
8107717
uniprot
proteins
pubmed
9642238
uniprot
proteins
pubmed
9858242
uniprot
proteins
sequence_length
587
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14643893}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000269|PubMed:14643893}.; SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion inner membrane {ECO:0000269|PubMed:14643893}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000269|PubMed:14643893}.
uniprot
proteins