Reviewed, UniProtKB/Swiss-Prot Q3ZC31 (HEM0_BOVIN)

Names and origin

Protein names

Recommended name:
    5-aminolevulinate synthase, erythroid-specific, mitochondrial
    EC=2.3.1.37
Alternative name(s):
    5-aminolevulinic acid synthase
    Delta-aminolevulinate synthase
    Delta-ALA synthetase
      Short name=ALAS-E

Gene names

Name:

ALAS2

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	587 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 By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Miscellaneous	There are two delta-ALA synthetase 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
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to hypoxia Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial inner membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5-aminolevulinate synthase activity Inferred from sequence or structural similarity. Source: UniProtKB 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 – ?49	49	Mitochondrion Potential
	Chain	?50 – 587	538	5-aminolevulinate synthase, erythroid-specific, mitochondrial		PRO_0000280705
Amino acid modifications
	Modified residue	391	1	N6-(pyridoxal phosphate)lysine Probable

Sequences

	Sequence		Length	Mass (Da)
	Q3ZC31-1 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: 8D0D94383137F5DC	FASTA	587	65,137
	10 20 30 40 50 60 MVTAAMLLQR CPVLIRSPTG LLGKMIKTHQ FLFGIGRCPI LATQGPSFSQ IHLKATKAGG 70 80 90 100 110 120 DSPSWAKSHC PFMLLELQDG KSKIVQKAAP EVQEDVKTFK TDLPTSLAST SLKKTFSSPQ 130 140 150 160 170 180 EPEKNSEKVT HLIQNNMAGD HVFGYDQFFR DKIMEKKQDH TYRVFKTVNR WADAYPFAEH 190 200 210 220 230 240 FFEASVASKD VSVWCSNDYL GMSRHPRVLQ ATQEILQRHG AGAGGTRNIS GTSKFHVELE 250 260 270 280 290 300 QELAELHQKD SALLFSSCFV ANDSTLFTLA KILPGCEIYS DAGNHASMIQ GIRNSGAAKF 310 320 330 340 350 360 VFRHNDPDHL KKLLKKSNPE TPKIVAFETV HSMDGAICPL EELCDVAHQY GALTFVDEVH 370 380 390 400 410 420 AVGLYGSRGA GIGERDGIMH KIDIISGTLG KAFGCVGGYI ASTRDLVDMV RSYAAGFIFT 430 440 450 460 470 480 TSLPPMVLSG ALESVRLLKG EEGQALRRAH QRNVKHMRQL LMDRGLPVIP CPSHIIPIRV 490 500 510 520 530 540 GDAMLNTRIC DLLLSKYGIY VQAINYPTVP RGEELLRLAP SPHHSPQMME DFVEKLLEAW 550 560 570 580 TEVGLPLQDI SIAACNFCRR PVHFELMSEW ERSYFGNMGP QYVTTYA

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC102938 mRNA. Translation: AAI02939.1.
IPI	IPI00707059.
RefSeq	NP_001030275.1.
UniGene	Bt.49467
3D structure databases
SMR	Q3ZC31. Positions 1-49.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000013178. Bos taurus. [Contig view]
GeneID	511791.
KEGG	bta:511791.
Phylogenomic databases
HOVERGEN	Q3ZC31.
OMA	Q3ZC31. DVSMAAC.
Enzyme and pathway databases
BRENDA	2.3.1.37. 251.
Family and domain databases
InterPro	IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR015118. 5aminolev_synth_preseq. IPR004839. Aminotrans_I/II. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. PF09029. Preseq_ALAS. 1 hit. [Graphical view]
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM0_BOVIN

Accession

Primary (citable) accession number: Q3ZC31

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	September 27, 2005
Last modified:	June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)