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MT000023

UniProt Annotations

Entry Information

Gene Name	5'-aminolevulinate synthase 2
Protein Entry	HEM0_HUMAN
UniProt ID	P22557
Species	Human

Comments

Comment type	Description
Alternative Products	Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=P22557-1; Sequence=Displayed; Name=2; Synonyms=Delta4; IsoId=P22557-2; Sequence=VSP_042852; Note=Constitutes 35-45% of erythrocytes ALAS2 mRNAs. Catalytic activity is 70% of isoform 1 activity.; Name=3; Synonyms=F143M; IsoId=P22557-3; Sequence=VSP_042851, VSP_042853; Note=Catalytic activity is 80% of isoform 1 activity.; Name=4; IsoId=P22557-4; Sequence=VSP_047330, VSP_042852;
Catalytic Activity	Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2). {ECO:0000269\|PubMed:14643893}.
Cofactor	Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Disease	Anemia, sideroblastic, X-linked (XLSA) [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:21252495, ECO:0000269\|PubMed:21309041, ECO:0000269\|PubMed:8107717, ECO:0000269\|PubMed:9858242}. Note=The disease is caused by mutations 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 mutations 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}.
Miscellaneous	There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.
Pathway	Porphyrin-containing compound metabolism; protoporphyrin- IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Sequence Caution	Sequence=CAA39795.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Similarity	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
Subcellular Location	Mitochondrion matrix {ECO:0000269\|PubMed:14643893}.
Subunit	Homodimer. Interacts with SUCLA2. {ECO:0000269\|PubMed:14643893}.
Tissue Specificity	Erythroid specific.