[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1093/nar/14.24.10115; PubMed=3808948 [NCBI, ExPASy, EBI, Israel, Japan] Bishop T.R., Frelin L.P., Boyer S.H.; "Nucleotide sequence of rat liver delta-aminolevulinic acid dehydratase cDNA."; Nucleic Acids Res. 14:10115-10115(1986).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-45. PubMed=3502704 [NCBI, ExPASy, EBI, Israel, Japan] Bishop T.R., Cohen P.J., Boyer S.H., Noyes A.N., Frelin L.P.; "Isolation of a rat liver delta-aminolevulinate dehydrase (ALAD) cDNA clone: evidence for unequal ALAD gene dosage among inbred mouse strains."; Proc. Natl. Acad. Sci. U.S.A. 83:5568-5572(1986).
[4]	PROTEIN SEQUENCE OF 56-84 AND 200-209, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.

Comments

CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2 H₂O.
COFACTOR: Zinc.
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen III from 5-aminolevulinate: step 1/4 .
SUBUNIT: Homooctamer.
SIMILARITY: Belongs to the ALADH 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

X04959; CAA28621.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061806; AAH61806.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A24724; A24724.

NP_037031.1; -.

3D structure databases

HSSP

P13716; 1E51. [HSSP ENTRY / PDB]

P06214; 1-328.

PTM databases

P06214; -.

Organism-specific databases

RGD

2083; Alad.

Gene expression databases

GermOnline

ENSRNOG00000015206; Rattus norvegicus.

Ontologies

GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006783;	Biological process: heme biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001731; 4pyrrol_synth_porphobiln_synth.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11458; AlaD_dehydratase; 1.

Pfam

PF00490; ALAD; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001415; Porphbilin_synth; 1.

PRINTS

PR00144; DALDHYDRTASE.

ProDom

PD002304; AlaD_dehydratase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00169; D_ALA_DEHYDRATASE; 1.

Genome annotation databases

Ensembl

ENSRNOG00000015206; Rattus norvegicus. [Contig view]

GeneID

25374; -.

KEGG

rno:25374; -.

NMPDR

fig|10116.3.peg.23271; -.

Phylogenomic databases

HOVERGEN

P06214; -.

Other

NextBio

606397; -.

UniRef

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

Keywords

Direct protein sequencing; Heme biosynthesis; Lyase; Metal-binding; Porphyrin biosynthesis; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 330`	`330`	`Delta-aminolevulinic acid dehydratase.`	`PRO_0000140530`
`ACT_SITE`	`252 252`		`By similarity.`
`METAL`	`122 122`		`Zinc; catalytic (By similarity).`
`METAL`	`124 124`		`Zinc; catalytic (By similarity).`
`METAL`	`132 132`		`Zinc; catalytic (By similarity).`

Sequence information

Length: 330 AA [This is the length of the unprocessed precursor]

Molecular weight: 36032 Da [This is the MW of the unprocessed precursor]

CRC64: 617F6E85B647AB25 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHHQSVLHSG YFHPLLRAWQ TTPSTVSATN LIYPIFVTDV PDDVQPIASL PGVARYGVNQ 

        70         80         90        100        110        120 
LEEMLRPLVE AGLRCVLIFG VPSRVPKDEQ GSAADSEDSP TIEAVRLLRK TFPTLLVACD 

       130        140        150        160        170        180 
VCLCPYTSHG HCGLLSENGA FLAEESRQRL AEVALAYAKA GCQVVAPSDM MDGRVEAIKA 

       190        200        210        220        230        240 
ALLKHGLGNR VSVMSYSAKF ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVAR 

       250        260        270        280        290        300 
DIQEGADILM VKPGLPYLDM VQEVKDKHPE LPLAVYQVSG EFAMLWHGAK AGAFDLRTAV 

       310        320        330 
LESMTAFRRA GADIIITYFA PQLLKWLKEE

P06214 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