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Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei280 – 2801Schiff-base intermediate with substrateBy similarity
Binding sitei290 – 2901Substrate 1By similarity
Binding sitei302 – 3021Substrate 1By similarity
Metal bindingi318 – 3181MagnesiumBy similarity
Active sitei333 – 3331Schiff-base intermediate with substrateBy similarity
Binding sitei359 – 3591Substrate 2By similarity
Binding sitei398 – 3981Substrate 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Chlorophyll biosynthesis, Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase, chloroplastic (EC:4.2.1.24)
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:HEMB
Synonyms:ALAD
OrganismiGlycine max (Soybean) (Glycine hispida)
Taxonomic identifieri3847 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
ProteomesiUP000008827 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4848ChloroplastSequence AnalysisAdd
BLAST
Chaini49 – 412364Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013320Add
BLAST

Proteomic databases

ProMEXiP43210.

Expressioni

Tissue specificityi

Leaves and root nodules.

Gene expression databases

GenevestigatoriP43210.

Interactioni

Subunit structurei

Homooctamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP43210.
SMRiP43210. Positions 88-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiP43210.
KOiK01698.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43210-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSIPNAPS AFNSQSYVGL RAPLRTFNFS SPQAAKIPRS QRLFVVRASD
60 70 80 90 100
SEFEAAVVAG KVPPAPPVRP RPAAPVGTPV VPSLPLHRRP RRNRKSPALR
110 120 130 140 150
SAFQETSISP ANFVYPLFIH EGEEDTPIGA MPGCYRLGWR HGLVEEVAKA
160 170 180 190 200
RDVGVNSVVL FPKIPDALKS PTGDEAYNEN GLVPRTIRLL KDKYPDLVIY
210 220 230 240 250
TDVALDPYSS DGHDGIVRED GVIMNDETVH QLCKQAVAQA QAGADVVSPS
260 270 280 290 300
DMMDGRVGAL RAALDAEGFQ HVSIMSYTAK YASSFYGPFR EALDSNPRFG
310 320 330 340 350
DKKTYQMNPA NYREALTEMR EDESEGADIL LVKPGLPYLD IIRLLRDNSP
360 370 380 390 400
LPIAAYQVSG EYAMIKAAGA LKMIDEEKVM MESLMCLRRA GADIILTYSA
410
LQAARCLCGE KR
Length:412
Mass (Da):45,068
Last modified:November 1, 1995 - v1
Checksum:i0ECDF209A09572D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04525 mRNA. Translation: AAA18342.1.
PIRiT06351.
RefSeqiNP_001238737.1. NM_001251808.1.
UniGeneiGma.6038.

Genome annotation databases

GeneIDi548095.
KEGGigmx:548095.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04525 mRNA. Translation: AAA18342.1.
PIRiT06351.
RefSeqiNP_001238737.1. NM_001251808.1.
UniGeneiGma.6038.

3D structure databases

ProteinModelPortaliP43210.
SMRiP43210. Positions 88-407.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

ProMEXiP43210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi548095.
KEGGigmx:548095.

Phylogenomic databases

InParanoidiP43210.
KOiK01698.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Gene expression databases

GenevestigatoriP43210.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiHEM2_SOYBN
AccessioniPrimary (citable) accession number: P43210
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 29, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.