UniProt Accession

 HEM2_MOUSE; P10518; Q3THV6 

Genbank Protein ID

 X13752; AK032908; AK167673; AK168119; AK168132; BC055930 

Genbank Nucleotide ID

 CAA32015.1; BAC28080.1; BAE39722.1; BAE40090.1; BAE40101.1; AAH55930.1 

Protein Name

 Delta-aminolevulinic acid dehydratase 

Protein Synonyms/Alias

 ALADH; Porphobilinogen synthase 

Gene Name

 Alad 

Gene Synonyms/Alias

 Lv 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
87	GVPSRVPKDEQGSAA	ubiquitination	[1]
179	DGRVEAIKAALLKHG	acetylation	[2]
179	DGRVEAIKAALLKHG	ubiquitination	[1]
184	AIKAALLKHGLGNRV	acetylation	[2]
184	AIKAALLKHGLGNRV	ubiquitination	[1]
199	SVMSYSAKFASCFYG	acetylation	[3]
199	SVMSYSAKFASCFYG	succinylation	[3]
252	GADMLMVKPGLPYLD	acetylation	[3, 4]
252	GADMLMVKPGLPYLD	succinylation	[3]
252	GADMLMVKPGLPYLD	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 

Functional Description

 Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). 

Sequence Annotation

 ACT_SITE 199 199 Schiff-base intermediate with substrate
 ACT_SITE 252 252 Schiff-base intermediate with substrate
 METAL 122 122 Zinc 1; catalytic (By similarity).
 METAL 124 124 Zinc 1; catalytic (By similarity).
 METAL 131 131 Zinc 2 (By similarity).
 METAL 132 132 Zinc 1; catalytic (By similarity).
 METAL 223 223 Zinc 2 (By similarity).
 BINDING 209 209 Substrate 1 (By similarity).
 BINDING 221 221 Substrate 1 (By similarity).
 BINDING 279 279 Substrate 2 (By similarity).
 BINDING 318 318 Substrate 2 (By similarity).  

Keyword

 3D-structure; Allosteric enzyme; Complete proteome; Heme biosynthesis; Lyase; Metal-binding; Porphyrin biosynthesis; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 330 AA 

Protein Sequence

Gene Ontology

 GO:0032791; F:lead ion binding; ISS:UniProtKB.
 GO:0004655; F:porphobilinogen synthase activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
 GO:0006783; P:heme biosynthetic process; ISS:UniProtKB.
 GO:0051260; P:protein homooligomerization; IEA:Compara.
 GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. 

Interpro

 IPR013785; Aldolase_TIM.
 IPR001731; Porphobilinogen_synth. 

Pfam

 PF00490; ALAD 

SMART

 SM01004; ALAD 

PROSITE

 PS00169; D_ALA_DEHYDRATASE 

PRINTS

 PR00144; DALDHYDRTASE.