P18080 (HEM0_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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
Synonyms:	ALASE

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.
Cofactor	Pyridoxal phosphate.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Subunit structure	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.

Ontologies

Keywords
Biological process	Heme biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5-aminolevulinate synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 18	18	Mitochondrion Potential
	Chain	19 – 513	495	5-aminolevulinate synthase, erythroid-specific, mitochondrial		PRO_0000001226
Amino acid modifications
	Modified residue	323	1	N6-(pyridoxal phosphate)lysine Probable

Sequences

	Sequence		Length	Mass (Da)
	P18080 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: C319A4DE5294CF74	FASTA	513	54,778
	10 20 30 40 50 60 MAAFLRCPLL ARHPPLARAF ATGARCPFMG FAHRAAPELQ EDVERPQIPA VEVLEELLRD 70 80 90 100 110 120 GGAALNRTVR DCMDEDAFPY EEQFQAQLGA LRRTHTYRVV TAVGRRADAP PLGTRGTAPH 130 140 150 160 170 180 TSVELWCSSD YLGLSRHPAV LRAARAALDA HGLGAGGTRN IGGTSPLHGA LERALALLHR 190 200 210 220 230 240 QPRAALFSSC FAANDTALDT LARILPGCQV YSDAGNHASM IQGIRRRGVP KFIFRHNDPH 250 260 270 280 290 300 HLEQLLGRSP PGVPKIVAFE SLHSMDGSIA PLEELCDVAH AYGALTFVDE VHAVGLYGAR 310 320 330 340 350 360 GAGIAERDGV QHKVDVVSGT LGKALGAVGG YIAGSEALVD AVRSLGPGFI FTTALPPQRG 370 380 390 400 410 420 GGALAALQVV GSAEGAALRR AHQRHAKHLR VLLRDRGLPA LPSHIVPVRW DAEANTRLSR 430 440 450 460 470 480 ALLEEHGLYV QAINHPTVPR GQELLLRIAP TPHHSPPMLE NLADKLSECW GAVGLPREDP 490 500 510 PGPSCSSCHR PLHLSLLSPL ERDQFGVRGA AAG

References

[1]	"Expression of delta-aminolevulinate synthase in avian cells: separate genes encode erythroid-specific and nonspecific isozymes." Riddle R.D., Yamamoto M., Engel J.D. Proc. Natl. Acad. Sci. U.S.A. 86:792-796(1989) [PubMed: 2915978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Erythroid cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M24367 mRNA. Translation: AAA20400.1.
IPI	IPI00572801.
PIR	SYCHLE. A31452.
3D structure databases
ProteinModelPortal	P18080.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG005954.
PhylomeDB	P18080.
Family and domain databases
InterPro	IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM0_CHICK

Accession

Primary (citable) accession number: P18080

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1995
Last modified:	September 21, 2011
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program