P24493 (HEM2_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Porphobilinogen synthase

Gene names

Name:	HEMB
Synonyms:	ALA1

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer By similarity.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the ALADH family.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Heme biosynthesis Porphyrin biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW porphobilinogen synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 56	56	Chloroplast Ref.1
	Chain	57 – 433	377	Delta-aminolevulinic acid dehydratase, chloroplastic		PRO_0000013321
Sites
	Active site	301	1	Schiff-base intermediate with substrate By similarity
	Active site	354	1	Schiff-base intermediate with substrate By similarity
	Metal binding	339	1	Magnesium By similarity
	Binding site	311	1	Substrate 1 By similarity
	Binding site	323	1	Substrate 1 By similarity
	Binding site	380	1	Substrate 2 By similarity
	Binding site	419	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P24493 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 4B02E3EFC4BBE131	FASTA	433	47,322
	10 20 30 40 50 60 MASTFNIPCN AGTIKNFNNS QRNLGFSSNL GINFAKTRFS NCGDSGRIPS QLVVRASERR 70 80 90 100 110 120 DNLTQQKTGL SIEECEAAVV AGNAPSAPPV PPTPKAPSGT PSVSPLSLGR RPRRNRTSPV 130 140 150 160 170 180 FRAAFQETTL SPANVVYPLF IHEGEEDTPI GAMPGCYRLG WRHGLVEEVA KARDVVVNSI 190 200 210 220 230 240 VVFPKPDALK SPTGDEAYNE NGLVPRTIRM LKDKFPDLII YTDVALDPYY YDGHDGIVTQ 250 260 270 280 290 300 HGVIMNDETV HQLCKQAVAQ ARAGADVVSP SDMMDGRVGA IRAALDAEGY SNVSIMSYTA 310 320 330 340 350 360 KYASSFYGPF REALDSNPRF GDKKTYQMNP ANYREALIET QEDESEGADI LLVKPGLPYL 370 380 390 400 410 420 DIIRLLRDNS DLPIAAYQVS GEYSMIKAGG VLKMIDEEKV MLESLLCLRR AGADIILTYF 430 ALQAARCLCG EKR

References

[1]	"Characterization of plastid 5-aminolevulinate dehydratase (ALAD; EC 4.2.1.24) from spinach (Spinacia oleracea L.) by sequencing and comparison with non-plant ALAD enzymes." Schaumburg A., Schneider-Poetsch H.A.W., Eckerskorn C. Z. Naturforsch. C 47:77-84(1992) [PubMed: 1351729] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-70. Strain: cv. Aestivato.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57842 mRNA. Translation: CAA40974.1.
PIR	A50000.
3D structure databases
ProteinModelPortal	P24493.
SMR	P24493. Positions 110-428.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11458. AlaD_dehydratase. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
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_SPIOL

Accession

Primary (citable) accession number: P24493

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program