Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P30124

- HEM2_PEA

UniProt

P30124 - HEM2_PEA

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell

    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 ALADH 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

    HTFVDLKSPF TLSNYLSFSS SKRRQPPSLF TVRASDSDFE AAVVAGKVPE    50
    APPVPPTPAS PAGTPVVPSL PIQRRPRRNR RSPALRSAFQ ETTLSPANFV 100
    YPLFIHEGEE DTPIGAMPGC YRLGWRHGLL EEVAKARDVG VNSVVLFPKI 150
    PDALKTPTGD EAYNEDGLVP RSIRLLKDKY PDLIIYTDVA LDPYSSDGHD 200
    GIVREDGVIM NDETVHQLCK QAVAQARAGA DVVSPSDMMD GRVGAMRVAL 250
    DAEGFQHVSI MSYTAKYASS FYGPFREALD SNPRFGDKKT YQMNPANYRE 300
    ALTEMREDES EGADILLVKP GLPYLDIIRL LRDNSPLPIA AYQVSGEYSM 350
    IKAGGALKMI DEEKVMMESL LCLRRAGADI ILTYFALQAA RTLCGEKR 398
    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 1, 2014
    This is version 79 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