Reviewed, UniProtKB/Swiss-Prot Q5R557 (HEM0_PONAB)

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

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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 protein 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.
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 By similarity
	Chain	50 – 587	538	5-aminolevulinate synthase, erythroid-specific, mitochondrial		PRO_0000290199
Amino acid modifications
	Modified residue	391	1	N6-(pyridoxal phosphate)lysine

Sequences

	Sequence		Length	Mass (Da)
	Q5R557-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: A4DF78C6271D0451	FASTA	587	64,648
	10 20 30 40 50 60 MVTAAMLLQC CPVPARGPTS LLGKVVKTHQ FLFGIGRCPI LATQGPNCSQ IHLKATKAGG 70 80 90 100 110 120 DSPSWAKGHC PFMLSELQDG KSKIVQKAAP EVQEDVKAFK TDLPSSLVSA SLKKPFSSPQ 130 140 150 160 170 180 EQEQISGKVT HLIQDNMPGN YVFSYDQFFR DKIMEKKQDH TYRVFKTVNR WADAYPFAQH 190 200 210 220 230 240 FSEASVASKD VSVWCSNDYL GMSRHPQVLR ATQETLQRHG AGAGGTRNIS GTSKFHVELE 250 260 270 280 290 300 QELAELHQKD SALLFSSCFV ANDSTLFTLA KILPGCEIYS DAGNHASMIQ GIRNSGAAKF 310 320 330 340 350 360 VFRHNDPDHL KKLLEKSNPK IPKIVAFEAV HSMDGAICPL EELCDVSHQY 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 GNAALNSKLC DLLLSKHGIY VQAINYPTVP RGEELLRLAP SPHHSPQMME DFVEKLLLAW 550 560 570 580 TEVGLPLQDV SVAACNFCRR PVHFELMSEW ERSYFGNMGP QYVTTYA

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR861013 mRNA. Translation: CAH93109.1.
RefSeq	NP_001127630.1.
UniGene	Pab.3363
3D structure databases
SMR	Q5R557. Positions 1-49.
ModBase	Search...
Genome annotation databases
GeneID	100174709.
Organism-specific databases
CTD	100174709.
Phylogenomic databases
HOVERGEN	Q5R557.
Enzyme and pathway databases
BRENDA	2.3.1.37. 269192.
Family and domain databases
InterPro	IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR015118. 5aminolev_synth_preseq. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. 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_PONAB

Accession

Primary (citable) accession number: Q5R557

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	December 21, 2004
Last modified:	September 22, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)