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P30124 (HEM2_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length398 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Plastidchloroplast.

Sequence similarities

Belongs to the ALADH family.

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Heme biosynthesis
Porphyrin biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termAllosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

porphobilinogen synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – ?Chloroplast
Chain? – 398Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013317

Sites

Active site2661Schiff-base intermediate with substrate By similarity
Active site3191Schiff-base intermediate with substrate By similarity
Metal binding3041Magnesium By similarity
Binding site2761Substrate 1 By similarity
Binding site2881Substrate 1 By similarity
Binding site3451Substrate 2 By similarity
Binding site3841Substrate 2 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P30124 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 75DDCB55CE3C6BD1

FASTA39843,815
        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 

« Hide

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, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M71235 mRNA. Translation: AAA33640.1.
PIRA40966.

3D structure databases

ProteinModelPortalP30124.
SMRP30124. Positions 74-393.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP30124.
ProMEXP30124.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00251; UER00318.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_PEA
AccessionPrimary (citable) accession number: P30124
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways