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P30124

- HEM2_PEA

UniProt

P30124 - HEM2_PEA

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Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Pisum sativum (Garden pea)
Status
Reviewed - 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

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

Pathwayi

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

  1. metal ion binding Source: UniProtKB-KW
  2. porphobilinogen synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-KW
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
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

  1. chloroplast Source: UniProtKB-KW
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.
ProMEXiP30124.

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.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[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:
EMBL
GenBank
DDBJ
Links Updated
M71235 mRNA. Translation: AAA33640.1.
PIRiA40966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M71235 mRNA. Translation: AAA33640.1 .
PIRi A40966.

3D structure databases

ProteinModelPortali P30124.
SMRi P30124. Positions 74-393.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P30124.
ProMEXi P30124.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view ]
PANTHERi PTHR11458. PTHR11458. 1 hit.
Pfami PF00490. ALAD. 1 hit.
[Graphical view ]
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 80 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