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P24493 (HEM2_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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=ALAD
Short name=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:HEMB
Synonyms:ALA1
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
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 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-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.

Subunit structure

Homooctamer By similarity.

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 peptide1 – 5656Chloroplast Ref.1
Chain57 – 433377Delta-aminolevulinic acid dehydratase, chloroplastic
PRO_0000013321

Sites

Active site3011Schiff-base intermediate with substrate By similarity
Active site3541Schiff-base intermediate with substrate By similarity
Metal binding3391Magnesium By similarity
Binding site3111Substrate 1 By similarity
Binding site3231Substrate 1 By similarity
Binding site3801Substrate 2 By similarity
Binding site4191Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P24493 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 4B02E3EFC4BBE131

FASTA43347,322
        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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-70.
Strain: cv. Aestivato.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57842 mRNA. Translation: CAA40974.1.
PIRA50000.

3D structure databases

ProteinModelPortalP24493.
SMRP24493. Positions 110-428.
ModBaseSearch...
MobiDBSearch...

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_SPIOL
AccessionPrimary (citable) accession number: P24493
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 83 of the entry and version 2 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