P30124 (HEM2_PEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Porphobilinogen synthase

Gene names

Name:	HEMB
Synonyms:	ALAD

Organism

Pisum sativum (Garden pea)

Taxonomic identifier

3888 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	398 AA.
Sequence status	Fragment.
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. Ref.2
Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O. Ref.2
Cofactor	Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator. Ref.2
Enzyme regulation	Activated by magnesium. Inhibited by succinyl acetone. Enzyme activity may depend on the oligomerization state, where the fully active octamer may dissociate and reassemble into less active lower oligomers. Ref.2
Pathway	Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer; formed by oligomerization of dimers. Probably forms also lower oligomers. Ref.2
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 protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – ?		Chloroplast
	Chain	? – 398		Delta-aminolevulinic acid dehydratase, chloroplastic		PRO_0000013317
Sites
	Active site	266	1	Schiff-base intermediate with substrate By similarity
	Active site	319	1	Schiff-base intermediate with substrate By similarity
	Metal binding	304	1	Magnesium By similarity
	Binding site	276	1	Substrate 1 By similarity
	Binding site	288	1	Substrate 1 By similarity
	Binding site	345	1	Substrate 2 By similarity
	Binding site	384	1	Substrate 2 By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P30124 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 75DDCB55CE3C6BD1	FASTA	398	43,815
	10 20 30 40 50 60 HTFVDLKSPF TLSNYLSFSS SKRRQPPSLF TVRASDSDFE AAVVAGKVPE APPVPPTPAS 70 80 90 100 110 120 PAGTPVVPSL PIQRRPRRNR RSPALRSAFQ ETTLSPANFV YPLFIHEGEE DTPIGAMPGC 130 140 150 160 170 180 YRLGWRHGLL EEVAKARDVG VNSVVLFPKI PDALKTPTGD EAYNEDGLVP RSIRLLKDKY 190 200 210 220 230 240 PDLIIYTDVA LDPYSSDGHD GIVREDGVIM NDETVHQLCK QAVAQARAGA DVVSPSDMMD 250 260 270 280 290 300 GRVGAMRVAL DAEGFQHVSI MSYTAKYASS FYGPFREALD SNPRFGDKKT YQMNPANYRE 310 320 330 340 350 360 ALTEMREDES EGADILLVKP GLPYLDIIRL LRDNSPLPIA AYQVSGEYSM IKAGGALKMI 370 380 390 DEEKVMMESL LCLRRAGADI ILTYFALQAA RTLCGEKR

References

[1]

"Aminolevulinic acid dehydratase in pea (Pisum sativum L.). Identification of an unusual metal-binding domain in the plant enzyme." Boese Q.F., Spano A.J., Li J., Timko M.P. J. Biol. Chem. 266:17060-17066(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

[2]

"Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions." Kervinen J., Dunbrack R.L. Jr., Litwin S., Martins J., Scarrow R.C., Volin M., Yeung A.T., Yoon E., Jaffe E.K. Biochemistry 39:9018-9029(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 70-75, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ENZYME REGULATION, MASS SPECTROMETRY, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M71235 mRNA. Translation: AAA33640.1.
PIR	A40966.
3D structure databases
ProteinModelPortal	P30124.
SMR	P30124. Positions 74-393.
ModBase	Search...
Proteomic databases
PRIDE	P30124.
ProMEX	P30124.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00251; UER00318.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
PANTHER	PTHR11458. PTHR11458. 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_PEA

Accession

Primary (citable) accession number: P30124

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program