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P43210 (HEM2_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:HEMB
Synonyms:ALAD
OrganismGlycine max (Soybean) (Glycine hispida) [Reference proteome]
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is committed to plant tetrapyrrole synthesis.

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.

Tissue specificity

Leaves and root nodules.

Sequence similarities

Belongs to the ALADH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Chloroplast Potential
Chain49 – 412364Delta-aminolevulinic acid dehydratase, chloroplastic
PRO_0000013320

Sites

Active site2801Schiff-base intermediate with substrate By similarity
Active site3331Schiff-base intermediate with substrate By similarity
Metal binding3181Magnesium By similarity
Binding site2901Substrate 1 By similarity
Binding site3021Substrate 1 By similarity
Binding site3591Substrate 2 By similarity
Binding site3981Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P43210 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 0ECDF209A09572D8

FASTA41245,068
        10         20         30         40         50         60 
MASSIPNAPS AFNSQSYVGL RAPLRTFNFS SPQAAKIPRS QRLFVVRASD SEFEAAVVAG 

        70         80         90        100        110        120 
KVPPAPPVRP RPAAPVGTPV VPSLPLHRRP RRNRKSPALR SAFQETSISP ANFVYPLFIH 

       130        140        150        160        170        180 
EGEEDTPIGA MPGCYRLGWR HGLVEEVAKA RDVGVNSVVL FPKIPDALKS PTGDEAYNEN 

       190        200        210        220        230        240 
GLVPRTIRLL KDKYPDLVIY TDVALDPYSS DGHDGIVRED GVIMNDETVH QLCKQAVAQA 

       250        260        270        280        290        300 
QAGADVVSPS DMMDGRVGAL RAALDAEGFQ HVSIMSYTAK YASSFYGPFR EALDSNPRFG 

       310        320        330        340        350        360 
DKKTYQMNPA NYREALTEMR EDESEGADIL LVKPGLPYLD IIRLLRDNSP LPIAAYQVSG 

       370        380        390        400        410 
EYAMIKAAGA LKMIDEEKVM MESLMCLRRA GADIILTYSA LQAARCLCGE KR 

« Hide

References

[1]"Plant delta-aminolevulinic acid dehydratase. Expression in soybean root nodules and evidence for a bacterial lineage of the Alad gene."
Kaczor C.M., Smith M.W., Sangwan I., O'Brian M.R.
Plant Physiol. 104:1411-1417(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04525 mRNA. Translation: AAA18342.1.
PIRT06351.
RefSeqNP_001238737.1. NM_001251808.1.
UniGeneGma.6038.

3D structure databases

ProteinModelPortalP43210.
SMRP43210. Positions 88-407.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

ProMEXP43210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID548095.
KEGGgmx:548095.

Phylogenomic databases

KOK01698.

Enzyme and pathway databases

UniPathwayUPA00251; UER00318.

Gene expression databases

GenevestigatorP43210.

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_SOYBN
AccessionPrimary (citable) accession number: P43210
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 83 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