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Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator.1 Publication

Enzyme regulationi

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.1 Publication

Pathway: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase, chloroplastic (HEMB)
  2. Porphobilinogen deaminase, chloroplastic (HEMC)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei266 – 2661Schiff-base intermediate with substrateBy similarity
Binding sitei276 – 2761Substrate 1By similarity
Binding sitei288 – 2881Substrate 1By similarity
Metal bindingi304 – 3041MagnesiumBy similarity
Active sitei319 – 3191Schiff-base intermediate with substrateBy similarity
Binding sitei345 – 3451Substrate 2By similarity
Binding sitei384 – 3841Substrate 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
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 398Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013317
Transit peptidei‹1 – ?Chloroplast

Proteomic databases

PRIDEiP30124.

Interactioni

Subunit structurei

Homooctamer; formed by oligomerization of dimers. Probably forms also lower oligomers.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP30124.
SMRiP30124. Positions 74-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Keywords - Domaini

Transit peptide

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: Fragment.

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

P30124-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
HTFVDLKSPF TLSNYLSFSS SKRRQPPSLF TVRASDSDFE AAVVAGKVPE
60 70 80 90 100
APPVPPTPAS PAGTPVVPSL PIQRRPRRNR RSPALRSAFQ ETTLSPANFV
110 120 130 140 150
YPLFIHEGEE DTPIGAMPGC YRLGWRHGLL EEVAKARDVG VNSVVLFPKI
160 170 180 190 200
PDALKTPTGD EAYNEDGLVP RSIRLLKDKY PDLIIYTDVA LDPYSSDGHD
210 220 230 240 250
GIVREDGVIM NDETVHQLCK QAVAQARAGA DVVSPSDMMD GRVGAMRVAL
260 270 280 290 300
DAEGFQHVSI MSYTAKYASS FYGPFREALD SNPRFGDKKT YQMNPANYRE
310 320 330 340 350
ALTEMREDES EGADILLVKP GLPYLDIIRL LRDNSPLPIA AYQVSGEYSM
360 370 380 390
IKAGGALKMI DEEKVMMESL LCLRRAGADI ILTYFALQAA RTLCGEKR
Length:398
Mass (Da):43,815
Last modified:April 1, 1993 - v1
Checksum:i75DDCB55CE3C6BD1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M71235 mRNA. Translation: AAA33640.1.
PIRiA40966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M71235 mRNA. Translation: AAA33640.1.
PIRiA40966.

3D structure databases

ProteinModelPortaliP30124.
SMRiP30124. Positions 74-393.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP30124.
ChEMBLiCHEMBL3286082.

Proteomic databases

PRIDEiP30124.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

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. "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.

Entry informationi

Entry nameiHEM2_PEA
AccessioniPrimary (citable) accession number: P30124
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 24, 2015
This is version 85 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, Direct protein sequencing

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.