Q55E06 (HEM2_DICDI) 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
Synonyms:	hemB
ORF Names:	DDB_G0269444

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 1 zinc ion per monomer By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer 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	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 – 333	333	Delta-aminolevulinic acid dehydratase		PRO_0000328039
Sites
	Active site	204	1	Schiff-base intermediate with substrate By similarity
	Active site	257	1	Schiff-base intermediate with substrate By similarity
	Metal binding	127	1	Zinc; catalytic By similarity
	Metal binding	129	1	Zinc; catalytic By similarity
	Metal binding	137	1	Zinc; catalytic By similarity
	Binding site	214	1	Substrate 1 By similarity
	Binding site	226	1	Substrate 1 By similarity
	Binding site	283	1	Substrate 2 By similarity
	Binding site	322	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55E06 [UniParc]. Last modified May 2, 2006. Version 2. Checksum: 6ADA07F1C4933E5F	FASTA	333	36,744
	10 20 30 40 50 60 MENNNKNYSH YLHSGYAHPI TRSWQGDKVI LKSQLIYPIF VTDLINTKTE IKSLPGQYQI 70 80 90 100 110 120 SSDLVVEFLR PLVEKGLKSI ILFGVIISGV KDEQASSADK RESSPVIKSI ELIKNEFPEI 130 140 150 160 170 180 LICTDLCLCA YTDHGHCGVL TEEGFIENEK SIIRLGEIAL SFAKAGAHVI APSDMMDCRV 190 200 210 220 230 240 GQIKKVLFQN GYGGRVAVMA YSSKFASSYY GPFRDAAGSG AKHGDRQAYQ LPIASRGLGL 250 260 270 280 290 300 RAALRDEAEG ADFIMVKPAG PYMDIIREVK DHVKVPVCCY QVSGEYAMIY HASVAGGIDL 310 320 330 KSGVMESLIS LQRSGCDIFI TYFTPQLLDW LKL

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000005 Genomic DNA. Translation: EAL72072.2.
RefSeq	XP_645975.2. XM_640883.2.
3D structure databases
HSSP	HSSP built from PDB template 1E51 based on UniProtKB P13716.
ProteinModelPortal	Q55E06.
SMR	Q55E06. Positions 9-332.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55E06.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231415; DDB0231415; DDB_G0269444.
GeneID	8616919.
GenomeReviews	Gene locus alad in contig CM000150_GR.
KEGG	ddi:DDB_G0269444.
Organism-specific databases
dictyBase	DDB_G0269444. hemB.
Phylogenomic databases
eggNOG	KOG2794.
GeneTree	EPrGT00050000005791.
HOGENOM	HBG285270.
OMA	GAHCVAP.
PhylomeDB	Q55E06.
ProtClustDB	CLSZ2432714.
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_DICDI

Accession

Primary (citable) accession number: Q55E06

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 2, 2006
Last modified:	January 25, 2012
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)