[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Liver; DOI=10.1093/nar/14.3.1379; PubMed=3005973 [NCBI, ExPASy, EBI, Israel, Japan] Maguire D.J., Day A.R., Borthwick I.A., Srivastava G., Wigley P.L., May B.K., Elliott W.H.; "Nucleotide sequence of the chicken 5-aminolevulinate synthase gene."; Nucleic Acids Res. 14:1379-1391(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=3839458 [NCBI, ExPASy, EBI, Israel, Japan] Borthwick I.A., Srivastava G., Day A.R., Pirola B.A., Snoswell M.A., May B.K., Elliott W.H.; "Complete nucleotide sequence of hepatic 5-aminolaevulinate synthase precursor."; Eur. J. Biochem. 150:481-484(1985).
[3]	NUCLEOTIDE SEQUENCE. PubMed=2915978 [NCBI, ExPASy, EBI, Israel, Japan] Riddle R.D., Yamamoto M., Engel J.D.; "Expression of delta-aminolevulinate synthase in avian cells: separate genes encode erythroid-specific and nonspecific isozymes."; Proc. Natl. Acad. Sci. U.S.A. 86:792-796(1989).

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: Homodimer.
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.
SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X02827; CAA26595.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03517; CAA27223.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03627; CAA27223.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A23538; SYCHAL.

NP_001018012.1; -.

3D structure databases

HSSP

P12998; 1BS0. [HSSP ENTRY / PDB]

ModBase

P07997.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0006783;	Biological process: heme biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR010961; 4pyrrol_synth_NH2levulA_synth.
IPR004839; Aminotrans_I/II.
IPR001917; Aminotrans_II_pyridoxalP_BS.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.

Pfam

PF00155; Aminotran_1_2; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01821; 5aminolev_synth; 1.

PROSITE

PS00599; AA_TRANSFER_CLASS_2; 1.

Genome annotation databases

GeneID

552895; -.

KEGG

gga:552895; -.

Phylogenomic databases

HOVERGEN

P07997; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Heme biosynthesis; Mitochondrion; Pyridoxal phosphate; Transferase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 56`	`56`	`Mitochondrion.`
`CHAIN`	`57 635`	`579`	`5-aminolevulinate synthase, nonspecific, mitochondrial.`	`PRO_0000001233`
`BINDING`	`440 440`		`Pyridoxal phosphate (covalent) (Probable).`
`CONFLICT`	`53 53`		`S -> A (in Ref. 2 and 3).`

Sequence information

Length: 635 AA [This is the length of the unprocessed precursor]

Molecular weight: 69948 Da [This is the MW of the unprocessed precursor]

CRC64: EEE708B85C1539BA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEAVVRRCPF LARVSQAFLQ KAGPSLLFYA QHCPKMMEAA PPAAARGLAT SASRGQQVEE 

        70         80         90        100        110        120 
TPAAQPEAKK AKEVAQQNTD GSQPPAGHPP AAAVQSSATK CPFLAAQMNH KSSNVFCKAS 

       130        140        150        160        170        180 
LELQEDVKEM QVDRKGKEFA KIPTNSVVRN TEAEGEEQSG LLKKFKDIML KQRPESVSHL 

       190        200        210        220        230        240 
LQDNLPKSVS TFQYDQFFEK KIDEKKKDHT YRVFKTVNRK AQIFPMADDY SDSLITKKEV 

       250        260        270        280        290        300 
SVWCSNDYLG MSRHPRVCGA VMDTLKQHGA GAGGTRNISG TSKFHVDLEK ELADLHGKDA 

       310        320        330        340        350        360 
ALLFSSCFVA NDSTLFTLAK MLPGCEIYSD SGNHASMIQG IRNSRVPKHI FRHNDVNHLR 

       370        380        390        400        410        420 
ELLKKSDPST PKIVAFETVH SMDGAVCPLE ELCDVAHEHG AITFVDEVHA VGLYGARGGG 

       430        440        450        460        470        480 
IGDRDGVMHK MDIISGTLGK AFACVGGYIS STSALIDTVR SYAAGFIFTT SLPPMLLAGA 

       490        500        510        520        530        540 
LESVRTLKSA EGQVLRRQHQ RNVKLMRQML MDAGLPVVHC PSHIIPIRVA DAAKNTEICD 

       550        560        570        580        590        600 
KLMSQHSIYV QAINYPTVPR GEELLRIAPT PHHTPQMMSY FLEKLLATWK DVGLELKPHS 

       610        620        630 
SAECNFCRRP LHFEVMSERE RSYFSGMSKL LSVSA

P07997 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools