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P24493

- HEM2_SPIOL

UniProt

P24493 - HEM2_SPIOL

Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

    2 5-aminolevulinate = porphobilinogen + 2 H2O.

    Cofactori

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei301 – 3011Schiff-base intermediate with substrateBy similarity
    Binding sitei311 – 3111Substrate 1By similarity
    Binding sitei323 – 3231Substrate 1By similarity
    Metal bindingi339 – 3391MagnesiumBy similarity
    Active sitei354 – 3541Schiff-base intermediate with substrateBy similarity
    Binding sitei380 – 3801Substrate 2By similarity
    Binding sitei419 – 4191Substrate 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:
    ALAD
    Short name:
    ALADH
    Alternative name(s):
    Porphobilinogen synthase
    Gene namesi
    Name:HEMB
    Synonyms:ALA1
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    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
    Transit peptidei1 – 5656Chloroplast1 PublicationAdd
    BLAST
    Chaini57 – 433377Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013321Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP24493.
    SMRiP24493. Positions 110-428.
    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: Complete.

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

    P24493-1 [UniParc]FASTAAdd to Basket

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    MASTFNIPCN AGTIKNFNNS QRNLGFSSNL GINFAKTRFS NCGDSGRIPS    50
    QLVVRASERR DNLTQQKTGL SIEECEAAVV AGNAPSAPPV PPTPKAPSGT 100
    PSVSPLSLGR RPRRNRTSPV FRAAFQETTL SPANVVYPLF IHEGEEDTPI 150
    GAMPGCYRLG WRHGLVEEVA KARDVVVNSI VVFPKPDALK SPTGDEAYNE 200
    NGLVPRTIRM LKDKFPDLII YTDVALDPYY YDGHDGIVTQ HGVIMNDETV 250
    HQLCKQAVAQ ARAGADVVSP SDMMDGRVGA IRAALDAEGY SNVSIMSYTA 300
    KYASSFYGPF REALDSNPRF GDKKTYQMNP ANYREALIET QEDESEGADI 350
    LLVKPGLPYL DIIRLLRDNS DLPIAAYQVS GEYSMIKAGG VLKMIDEEKV 400
    MLESLLCLRR AGADIILTYF ALQAARCLCG EKR 433
    Length:433
    Mass (Da):47,322
    Last modified:November 1, 1995 - v2
    Checksum:i4B02E3EFC4BBE131
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57842 mRNA. Translation: CAA40974.1.
    PIRiA50000.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57842 mRNA. Translation: CAA40974.1 .
    PIRi A50000.

    3D structure databases

    ProteinModelPortali P24493.
    SMRi P24493. Positions 110-428.
    ModBasei Search...
    MobiDBi Search...

    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. "Characterization of plastid 5-aminolevulinate dehydratase (ALAD; EC 4.2.1.24) from spinach (Spinacia oleracea L.) by sequencing and comparison with non-plant ALAD enzymes."
      Schaumburg A., Schneider-Poetsch H.A.W., Eckerskorn C.
      Z. Naturforsch. C 47:77-84(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-70.
      Strain: cv. Aestivato.

    Entry informationi

    Entry nameiHEM2_SPIOL
    AccessioniPrimary (citable) accession number: P24493
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 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