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P06214

- HEM2_RAT

UniProt

P06214 - HEM2_RAT

Protein

Delta-aminolevulinic acid dehydratase

Gene

Alad

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      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 8 zinc ions per octamer. Requires four zinc ions per octamer for full catalytic activity. Can bind up to 2 zinc ions per subunit By similarity.By similarity

    Enzyme regulationi

    Can alternate between a fully active homooctamer and a low-activity homohexamer. A bound magnesium ion may promote the assembly of the fully active homooctamer. The magnesium-binding site is absent in the low-activity homohexamer. Inhibited by compounds that favor the hexameric state. Inhibited by divalent lead ions. The lead ions partially displace the zinc cofactor By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi122 – 1221Zinc 1; catalyticBy similarity
    Metal bindingi124 – 1241Zinc 1; catalyticBy similarity
    Metal bindingi131 – 1311Zinc 2By similarity
    Metal bindingi132 – 1321Zinc 1; catalyticBy similarity
    Active sitei199 – 1991Schiff-base intermediate with substrateBy similarity
    Binding sitei209 – 2091Substrate 1By similarity
    Binding sitei221 – 2211Substrate 1By similarity
    Metal bindingi223 – 2231Zinc 2By similarity
    Active sitei252 – 2521Schiff-base intermediate with substrateBy similarity
    Binding sitei279 – 2791Substrate 2By similarity
    Binding sitei318 – 3181Substrate 2By similarity

    GO - Molecular functioni

    1. lead ion binding Source: UniProtKB
    2. porphobilinogen synthase activity Source: UniProtKB
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to lead ion Source: RGD
    2. heme biosynthetic process Source: UniProtKB
    3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    4. response to activity Source: RGD
    5. response to aluminum ion Source: RGD
    6. response to amino acid Source: RGD
    7. response to arsenic-containing substance Source: RGD
    8. response to cadmium ion Source: RGD
    9. response to cobalt ion Source: RGD
    10. response to drug Source: RGD
    11. response to ethanol Source: RGD
    12. response to fatty acid Source: RGD
    13. response to glucocorticoid Source: RGD
    14. response to herbicide Source: RGD
    15. response to hormone Source: RGD
    16. response to hypoxia Source: RGD
    17. response to inorganic substance Source: RGD
    18. response to ionizing radiation Source: RGD
    19. response to iron ion Source: RGD
    20. response to lead ion Source: RGD
    21. response to lipopolysaccharide Source: RGD
    22. response to mercury ion Source: RGD
    23. response to metal ion Source: RGD
    24. response to methylmercury Source: RGD
    25. response to nutrient Source: RGD
    26. response to nutrient levels Source: RGD
    27. response to organic cyclic compound Source: RGD
    28. response to organic substance Source: RGD
    29. response to oxidative stress Source: RGD
    30. response to platinum ion Source: RGD
    31. response to selenium ion Source: RGD
    32. response to toxic substance Source: RGD
    33. response to vitamin Source: RGD
    34. response to vitamin B1 Source: RGD
    35. response to vitamin E Source: RGD
    36. response to zinc ion Source: RGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00251; UER00318.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
    Short name:
    ALADH
    Alternative name(s):
    Porphobilinogen synthase
    Gene namesi
    Name:Alad
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 5

    Organism-specific databases

    RGDi2083. Alad.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. extracellular space Source: RGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 330330Delta-aminolevulinic acid dehydratasePRO_0000140530Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei199 – 1991N6-succinyllysineBy similarity
    Modified residuei215 – 2151PhosphoserineBy similarity
    Modified residuei252 – 2521N6-succinyllysineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP06214.
    PRIDEiP06214.

    PTM databases

    PhosphoSiteiP06214.

    Expressioni

    Gene expression databases

    GenevestigatoriP06214.

    Interactioni

    Subunit structurei

    Homooctamer; active form. Homohexamer; low activity form By similarity.By similarity

    Protein-protein interaction databases

    BioGridi247413. 1 interaction.
    MINTiMINT-4567662.
    STRINGi10116.ENSRNOP00000020625.

    Structurei

    3D structure databases

    ProteinModelPortaliP06214.
    SMRiP06214. Positions 5-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Phylogenomic databases

    eggNOGiCOG0113.
    GeneTreeiENSGT00390000006998.
    HOGENOMiHOG000020323.
    HOVERGENiHBG001222.
    InParanoidiP06214.
    KOiK01698.
    OMAiDHPTACY.
    OrthoDBiEOG751NFP.
    PhylomeDBiP06214.
    TreeFamiTF300665.

    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]
    PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
    PRINTSiPR00144. DALDHYDRTASE.
    SMARTiSM01004. ALAD. 1 hit.
    [Graphical view]
    PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06214-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHHQSVLHSG YFHPLLRAWQ TTPSTVSATN LIYPIFVTDV PDDVQPIASL    50
    PGVARYGVNQ LEEMLRPLVE AGLRCVLIFG VPSRVPKDEQ GSAADSEDSP 100
    TIEAVRLLRK TFPTLLVACD VCLCPYTSHG HCGLLSENGA FLAEESRQRL 150
    AEVALAYAKA GCQVVAPSDM MDGRVEAIKA ALLKHGLGNR VSVMSYSAKF 200
    ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVAR DIQEGADILM 250
    VKPGLPYLDM VQEVKDKHPE LPLAVYQVSG EFAMLWHGAK AGAFDLRTAV 300
    LESMTAFRRA GADIIITYFA PQLLKWLKEE 330
    Length:330
    Mass (Da):36,032
    Last modified:January 1, 1988 - v1
    Checksum:i617F6E85B647AB25
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04959 mRNA. Translation: CAA28621.1.
    BC061806 mRNA. Translation: AAH61806.1.
    PIRiA24724.
    RefSeqiNP_037031.1. NM_012899.2.
    XP_006238296.1. XM_006238234.1.
    XP_006238297.1. XM_006238235.1.
    UniGeneiRn.3941.

    Genome annotation databases

    EnsembliENSRNOT00000020625; ENSRNOP00000020625; ENSRNOG00000015206.
    GeneIDi25374.
    KEGGirno:25374.
    UCSCiRGD:2083. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04959 mRNA. Translation: CAA28621.1 .
    BC061806 mRNA. Translation: AAH61806.1 .
    PIRi A24724.
    RefSeqi NP_037031.1. NM_012899.2.
    XP_006238296.1. XM_006238234.1.
    XP_006238297.1. XM_006238235.1.
    UniGenei Rn.3941.

    3D structure databases

    ProteinModelPortali P06214.
    SMRi P06214. Positions 5-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247413. 1 interaction.
    MINTi MINT-4567662.
    STRINGi 10116.ENSRNOP00000020625.

    PTM databases

    PhosphoSitei P06214.

    Proteomic databases

    PaxDbi P06214.
    PRIDEi P06214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000020625 ; ENSRNOP00000020625 ; ENSRNOG00000015206 .
    GeneIDi 25374.
    KEGGi rno:25374.
    UCSCi RGD:2083. rat.

    Organism-specific databases

    CTDi 210.
    RGDi 2083. Alad.

    Phylogenomic databases

    eggNOGi COG0113.
    GeneTreei ENSGT00390000006998.
    HOGENOMi HOG000020323.
    HOVERGENi HBG001222.
    InParanoidi P06214.
    KOi K01698.
    OMAi DHPTACY.
    OrthoDBi EOG751NFP.
    PhylomeDBi P06214.
    TreeFami TF300665.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00318 .

    Miscellaneous databases

    NextBioi 606397.
    PROi P06214.

    Gene expression databases

    Genevestigatori P06214.

    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 ]
    PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
    PRINTSi PR00144. DALDHYDRTASE.
    SMARTi SM01004. ALAD. 1 hit.
    [Graphical view ]
    PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of rat liver delta-aminolevulinic acid dehydratase cDNA."
      Bishop T.R., Frelin L.P., Boyer S.H.
      Nucleic Acids Res. 14:10115-10115(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Prostate.
    3. "Isolation of a rat liver delta-aminolevulinate dehydrase (ALAD) cDNA clone: evidence for unequal ALAD gene dosage among inbred mouse strains."
      Bishop T.R., Cohen P.J., Boyer S.H., Noyes A.N., Frelin L.P.
      Proc. Natl. Acad. Sci. U.S.A. 83:5568-5572(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-45.
    4. Lubec G., Afjehi-Sadat L.
      Submitted (NOV-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 56-84 AND 200-209, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Spinal cord.

    Entry informationi

    Entry nameiHEM2_RAT
    AccessioniPrimary (citable) accession number: P06214
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, 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