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    ALAD aminolevulinate dehydratase [ Homo sapiens (human) ]

    Gene ID: 210, updated on 4-Sep-2016
    Official Symbol
    ALADprovided by HGNC
    Official Full Name
    aminolevulinate dehydrataseprovided by HGNC
    Primary source
    HGNC:HGNC:395
    See related
    Ensembl:ENSG00000148218 HPRD:00504; MIM:125270; Vega:OTTHUMG00000020522
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    PBGS; ALADH
    Summary
    The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. Alternative splicing of this gene results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2015]
    Orthologs
    Location:
    9q33.1
    Exon count:
    14
    Annotation release Status Assembly Chr Location
    108 current GRCh38.p7 (GCF_000001405.33) 9 NC_000009.12 (113386312..113401338, complement)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 9 NC_000009.11 (116148592..116163618, complement)

    Chromosome 9 - NC_000009.12Genomic Context describing neighboring genes Neighboring gene B-box and SPRY domain containing Neighboring gene haloacid dehalogenase like hydrolase domain containing 3 Neighboring gene chromosome 9 open reading frame 43 Neighboring gene DNA polymerase epsilon 3, accessory subunit Neighboring gene regulator of G-protein signaling 3 Neighboring gene uncharacterized LOC105376221

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    • Heme Biosynthesis, organism-specific biosystem (from WikiPathways)
      Heme Biosynthesis, organism-specific biosystemThe enzymatic process that produces heme is properly called porphyrin synthesis, as all the intermediates are tetrapyrroles that are chemically classified are porphyrins. The process is highly conser...
    • Heme biosynthesis, organism-specific biosystem (from REACTOME)
      Heme biosynthesis, organism-specific biosystemEight enzymes are involved in heme biosynthesis, four each in the mitochondria and the cytosol. The process starts in the mitochondria with the condensation of succinyl CoA (from the TCA cycle) and g...
    • Metabolic pathways, organism-specific biosystem (from KEGG)
      Metabolic pathways, organism-specific biosystem
      Metabolic pathways
    • Metabolism, organism-specific biosystem (from REACTOME)
      Metabolism, organism-specific biosystemMetabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as th...
    • Metabolism of porphyrins, organism-specific biosystem (from REACTOME)
      Metabolism of porphyrins, organism-specific biosystemPorphyrins are heterocyclic macrocycles, consisting of four pyrrole subunits (tetrapyrrole) linked by four methine (=CH-) bridges. The extensive conjugated porphyrin macrocycle is chromatic and the n...
    • Porphyrin and chlorophyll metabolism, organism-specific biosystem (from KEGG)
      Porphyrin and chlorophyll metabolism, organism-specific biosystem
      Porphyrin and chlorophyll metabolism
    • Porphyrin and chlorophyll metabolism, conserved biosystem (from KEGG)
      Porphyrin and chlorophyll metabolism, conserved biosystem
      Porphyrin and chlorophyll metabolism
    • heme biosynthesis, organism-specific biosystem (from BIOCYC)
      heme biosynthesis, organism-specific biosystemGeneral Background Heme (protoheme, heme b) is an iron-containing porphyrin, that belongs to the family of macrocyclic tetrapyrroles. It has a diverse range of biological functions as a prosthetic g...
    • superpathway of heme biosynthesis from glycine, conserved biosystem (from BIOCYC)
      superpathway of heme biosynthesis from glycine, conserved biosystemGeneral Background Heme (protoheme, heme b) is an iron-containing prosthetic group found in many essential proteins including cytochromes and heme-containing globins. In addition to its role in oxi...
    • tetrapyrrole biosynthesis, organism-specific biosystem (from BIOCYC)
      tetrapyrrole biosynthesis, organism-specific biosystemBackground Tetrapyrroles play a role in a variety of biological processes such as photosynthesis and respiration. They are large macrocyclic compounds derived from a common biosynthetic pathway . Te...
    • tetrapyrrole biosynthesis II (from glycine), conserved biosystem (from BIOCYC)
      tetrapyrrole biosynthesis II (from glycine), conserved biosystemTetrapyrrole compounds include four rings of the pyrrole type, generally linked together by single-atom bridges between the alpha positions of the five-membered pyrrole rings. Tetrapyrroles usually f...
    Products Interactant Other Gene Complex Source Pubs Description

    Markers

    Homology

    Clone Names

    • MGC5057

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    catalytic activity TAS
    Traceable Author Statement
    more info
    PubMed 
    identical protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    lead ion binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    porphobilinogen synthase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    porphobilinogen synthase activity TAS
    Traceable Author Statement
    more info
     
    zinc ion binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Process Evidence Code Pubs
    cellular response to interleukin-4 IEA
    Inferred from Electronic Annotation
    more info
     
    cellular response to lead ion IEA
    Inferred from Electronic Annotation
    more info
     
    heme biosynthetic process IDA
    Inferred from Direct Assay
    more info
    PubMed 
    heme biosynthetic process TAS
    Traceable Author Statement
    more info
     
    protein homooligomerization IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    protoporphyrinogen IX biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
     
    response to activity IEA
    Inferred from Electronic Annotation
    more info
     
    response to aluminum ion IEA
    Inferred from Electronic Annotation
    more info
     
    response to amino acid IEA
    Inferred from Electronic Annotation
    more info
     
    response to arsenic-containing substance IEA
    Inferred from Electronic Annotation
    more info
     
    response to cadmium ion IEA
    Inferred from Electronic Annotation
    more info
     
    response to cobalt ion IEA
    Inferred from Electronic Annotation
    more info
     
    response to drug IEA
    Inferred from Electronic Annotation
    more info
     
    response to ethanol IEA
    Inferred from Electronic Annotation
    more info
     
    response to fatty acid IEA
    Inferred from Electronic Annotation
    more info
     
    response to glucocorticoid IEA
    Inferred from Electronic Annotation
    more info
     
    response to herbicide IEA
    Inferred from Electronic Annotation
    more info
     
    response to hypoxia IEA
    Inferred from Electronic Annotation
    more info
     
    response to ionizing radiation IEA
    Inferred from Electronic Annotation
    more info
     
    response to iron ion IEA
    Inferred from Electronic Annotation
    more info
     
    response to lipopolysaccharide IEA
    Inferred from Electronic Annotation
    more info
     
    response to mercury ion IEA
    Inferred from Electronic Annotation
    more info
     
    response to methylmercury IEA
    Inferred from Electronic Annotation
    more info
     
    response to oxidative stress IEA
    Inferred from Electronic Annotation
    more info
     
    response to platinum ion IEA
    Inferred from Electronic Annotation
    more info
     
    response to selenium ion IEA
    Inferred from Electronic Annotation
    more info
     
    response to vitamin B1 IEA
    Inferred from Electronic Annotation
    more info
     
    response to vitamin E IEA
    Inferred from Electronic Annotation
    more info
     
    response to zinc ion IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    cytosol TAS
    Traceable Author Statement
    more info
     
    extracellular exosome IDA
    Inferred from Direct Assay
    more info
    PubMed 
    extracellular space IEA
    Inferred from Electronic Annotation
    more info
     
    nucleus IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Preferred Names
    delta-aminolevulinic acid dehydratase
    Names
    aminolevulinate, delta-, dehydratase
    porphobilinogen synthase
    testicular tissue protein Li 95
    NP_000022.3
    NP_001003945.1
    NP_001304674.1

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    Genomic

    1. NG_008716.1 RefSeqGene

      Range
      5001..20027
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_000031.5NP_000022.3  delta-aminolevulinic acid dehydratase isoform b

      See identical proteins and their annotated locations for NP_000022.3

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) lacks a segment of the coding region and initiates translation from an alternate start codon, compared to variant 1. The resulting isoform (b) has a distinct N-terminus, compared to isoform a.
      Source sequence(s)
      AK131490, AK290490, BC000977, BU625796, DA412142, DA805310
      Consensus CDS
      CCDS6794.2
      UniProtKB/Swiss-Prot
      P13716
      UniProtKB/TrEMBL
      A0A140VJL9, Q6ZMU0
      Related
      ENSP00000386284, OTTHUMP00000021953, ENST00000409155, OTTHUMT00000053724
      Conserved Domains (1) summary
      cd04824
      Location:8327
      eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...
    2. NM_001003945.2NP_001003945.1  delta-aminolevulinic acid dehydratase isoform a

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the longest transcript, and encodes the longest isoform (a).
      Source sequence(s)
      AK131490, AK290490, BU625796, DA412142
      UniProtKB/Swiss-Prot
      P13716
      UniProtKB/TrEMBL
      Q6ZMU0
      Conserved Domains (1) summary
      cd04824
      Location:68356
      eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...
    3. NM_001317745.1NP_001304674.1  delta-aminolevulinic acid dehydratase isoform c

      Status: REVIEWED

      Description
      Transcript Variant: This variant (3) differs in the 5' UTR, lacks an alternate in-frame exon in the 5' coding region and initiates translation from an alternate start codon, compared to variant 1. The resulting isoform (c) has a distinct N-terminus compared to isoform a.
      Source sequence(s)
      AK131490, AK295945, BU625796
      UniProtKB/TrEMBL
      B7Z3I9, Q6ZMU0
      Conserved Domains (1) summary
      cd04824
      Location:17319
      eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 108 details...Open this link in a new tab

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p7 Primary Assembly

    Genomic

    1. NC_000009.12 Reference GRCh38.p7 Primary Assembly

      Range
      113386312..113401338 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011518364.2XP_011516666.1  

      See identical proteins and their annotated locations for XP_011516666.1

      UniProtKB/Swiss-Prot
      P13716
      UniProtKB/TrEMBL
      A0A024R877
      Conserved Domains (1) summary
      cd04824
      Location:17336
      eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...

    Alternate CHM1_1.1

    Genomic

    1. NC_018920.2 Alternate CHM1_1.1

      Range
      116295230..116310254 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
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