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Q5R971

- HEM2_PONAB

UniProt

Q5R971 - HEM2_PONAB

Protein

Delta-aminolevulinic acid dehydratase

Gene

ALAD

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 2 (12 Apr 2005)
      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

    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. heme biosynthetic process Source: UniProtKB
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 330330Delta-aminolevulinic acid dehydratasePRO_0000140529Add
    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

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R971.
    SMRiQ5R971. Positions 1-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Phylogenomic databases

    HOVERGENiHBG001222.
    InParanoidiQ5R971.
    KOiK01698.

    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.

    Q5R971-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPQSVLHSG YFHPLLRAWQ TATTTLNASN LIYPIFVTDV PDDIQPIASL    50
    PGVARYGVNR LEEMLRPLVE EGLRCVLIFG VPSRVPKDER GSAADSEESP 100
    AIEAIHLLRK TFPNLLVACD VCLCPYTSHG HCGLLSENGA FQAEESRQRL 150
    AEVALAYAKA GCQVVAPSDM MDGRVEAIKE TLMAHGLGSR VSVMSYSAKF 200
    ASCFYGPFRD AAKSSPAFGD RRCYQLPPGA RGLALRAVDR DVREGADMLM 250
    VKPGMPYLDI VREVKDKHPD LPLAVYHVSG EFAMLWHGAQ AGAFDLKAAV 300
    LEAMTAFRRA GADIIITHYT PQLLQWLKEE 330
    Length:330
    Mass (Da):36,200
    Last modified:April 12, 2005 - v2
    Checksum:iBFCC5654B32A3FF3
    GO

    Sequence cautioni

    The sequence CAH91689.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859521 mRNA. Translation: CAH91689.1. Different initiation.
    RefSeqiNP_001127135.2. NM_001133663.2.

    Genome annotation databases

    GeneIDi100174182.
    KEGGipon:100174182.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859521 mRNA. Translation: CAH91689.1 . Different initiation.
    RefSeqi NP_001127135.2. NM_001133663.2.

    3D structure databases

    ProteinModelPortali Q5R971.
    SMRi Q5R971. Positions 1-328.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174182.
    KEGGi pon:100174182.

    Organism-specific databases

    CTDi 210.

    Phylogenomic databases

    HOVERGENi HBG001222.
    InParanoidi Q5R971.
    KOi K01698.

    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 ]
    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain cortex.

    Entry informationi

    Entry nameiHEM2_PONAB
    AccessioniPrimary (citable) accession number: Q5R971
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 58 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, 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