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P45623 (HEM2_SELMA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 70. 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:ALA2
OrganismSelaginella martensii (Martens's spike moss)
Taxonomic identifier3247 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaLycopodiophytaIsoetopsidaSelaginellalesSelaginellaceaeSelaginella

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 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
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 – 4040Chloroplast Potential
Chain41 – 417377Delta-aminolevulinic acid dehydratase, chloroplastic
PRO_0000013319

Sites

Active site2861Schiff-base intermediate with substrate By similarity
Active site3391Schiff-base intermediate with substrate By similarity
Metal binding3241Magnesium By similarity
Binding site2961Substrate 1 By similarity
Binding site3081Substrate 1 By similarity
Binding site3651Substrate 2 By similarity
Binding site4041Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P45623 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 036E57A607886759

FASTA41745,182
        10         20         30         40         50         60 
MAALLVPGGG AAPGLVWRRR RAAVQCAAAS PSSPDPSWRT NVVSDRVSVE PSPRTIHECE 

        70         80         90        100        110        120 
ADVVSGNPPA APAAPAKAKA PPGTPVVKPL RLTSRPRRNR KSAALRDAFQ ETTLTPANFI 

       130        140        150        160        170        180 
LPLFIHEGEE DSPIGAMPGC SRLGWRHGLI DEVYKARDVG VNSVVLFPKI PDALKSSTGD 

       190        200        210        220        230        240 
EAYNPDGLVP RAIRTLKDKF PDLVIYTDVA LDPYSSDGHD GIVREDGVIM NDETVHQLCK 

       250        260        270        280        290        300 
QAVAQAEAGA DVVSPSDMMD GRVGAIRTAL DEAGYYHVSI MAYTAKYASA FYEPFREELD 

       310        320        330        340        350        360 
SNPRFGDKKT YQMNPENYRE ALLEVHADES EGADILMVKP AMPYLHVIRL LRDTSALPIS 

       370        380        390        400        410 
AYQVSGEYSM IKAAASQGML DEKKAILESL LCIKRAGADV ILTYAALQAA RWLCGEK 

« Hide

References

[1]Sollbach M., Schneider-Poetsch H.A.W.
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75043 Genomic DNA. Translation: CAA52955.1.

3D structure databases

ProteinModelPortalP45623.
SMRP45623. Positions 94-413.
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_SELMA
AccessionPrimary (citable) accession number: P45623
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 70 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