Q58DK5 (HEM2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta-aminolevulinic acid dehydratase
Short name=ALADH
EC=4.2.1.24

Alternative name(s):
Porphobilinogen synthase

Gene names

Name:

ALAD

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	329 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O.
Cofactor	Binds 8 zinc ions per octamer. Only four zinc ions per octamer are required for full catalytic activity. Only four zinc ions per octamer are tightly bound. Can bind 2 zinc ions per subunit. The first zinc ion is important for catalysis By similarity.
Enzyme regulation	Can alternate between a fully active homooctamer and a low-activity homohexamer. A bound magnesium ion may promote the assembly of the fully active homooctamer. The magnesium-binding site is absent in the low-activity homohexamer. Inhibited by compounds that favor the hexameric state. Inhibited by divalent lead ions. The lead ions partially displace the zinc cofactor By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer; active form. Homohexamer; low activity form By similarity.
Sequence similarities	Belongs to the ALADH family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	lead ion binding Inferred from sequence or structural similarity. Source: UniProtKB porphobilinogen synthase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Delta-aminolevulinic acid dehydratase		PRO_0000328038
Sites
	Active site	199	1	Schiff-base intermediate with substrate By similarity
	Active site	252	1	Schiff-base intermediate with substrate By similarity
	Metal binding	122	1	Zinc 1; catalytic By similarity
	Metal binding	124	1	Zinc 1; catalytic By similarity
	Metal binding	131	1	Zinc 2 By similarity
	Metal binding	132	1	Zinc 1; catalytic By similarity
	Metal binding	223	1	Zinc 2 By similarity
	Binding site	209	1	Substrate 1 By similarity
	Binding site	221	1	Substrate 1 By similarity
	Binding site	279	1	Substrate 2 By similarity
	Binding site	318	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q58DK5 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 8BD0E141749B6465	FASTA	329	36,081
	10 20 30 40 50 60 MHPQSVLHSG YFHPLLRNWQ TAATSLSASN LIYPIFVTDV PDDKQPIASL PGVARYGVNR 70 80 90 100 110 120 LEEMLKPLVE EGLRCVLIFG VPSRVPKDER GSAADSEDSP AIEAIRLLRK NFPSLLVACD 130 140 150 160 170 180 VCLCPYTSHG HCGLLSENGS FQAEESRQRL AEVALAYAKA GCQVVAPSDM MDGRVEAIKE 190 200 210 220 230 240 ALMAHGFGNR VSVMSYSAKF ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVDR 250 260 270 280 290 300 DVREGADLLM VKPGTPYLDI VREVKNKHPE LPLAVYHVSG EFAMLWHGAQ AGAFDLKAAV 310 320 LEVMTAFRRA GADVIITYYT PQLLQWLKE

References

[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT021592 mRNA. Translation: AAX46439.1.
IPI	IPI00712730.
RefSeq	NP_001014895.1. NM_001014895.1.
UniGene	Bt.37574.
3D structure databases
HSSP	HSSP built from PDB template 1E51 based on UniProtKB P13716.
ProteinModelPortal	Q58DK5.
SMR	Q58DK5. Positions 1-328.
ModBase	Search...
Protein-protein interaction databases
STRING	Q58DK5.
Proteomic databases
PRIDE	Q58DK5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000000315; ENSBTAP00000000315; ENSBTAG00000000251.
GeneID	510679.
KEGG	bta:510679.
Organism-specific databases
CTD	210.
Phylogenomic databases
GeneTree	ENSGT00390000006998.
HOVERGEN	HBG001222.
InParanoid	Q58DK5.
OrthoDB	EOG4BRWM1.
PhylomeDB	Q58DK5.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01698.
PANTHER	PTHR11458. AlaD_dehydratase. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PIRSF	PIRSF001415. Porphbilin_synth. 1 hit.
PRINTS	PR00144. DALDHYDRTASE.
SMART	SM01004. ALAD. 1 hit. [Graphical view]
PROSITE	PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM2_BOVIN

Accession

Primary (citable) accession number: Q58DK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program