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P10518

- HEM2_MOUSE

UniProt

P10518 - HEM2_MOUSE

Protein

Delta-aminolevulinic acid dehydratase

Gene

Alad

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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. identical protein binding Source: MGI
    2. lead ion binding Source: UniProtKB
    3. porphobilinogen synthase activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to interleukin-4 Source: MGI
    2. heme biosynthetic process Source: UniProtKB
    3. protein homooligomerization Source: Ensembl
    4. 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

    ReactomeiREACT_203298. Heme biosynthesis.
    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
    Synonyms:Lv
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:96853. Alad.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 330330Delta-aminolevulinic acid dehydratasePRO_0000140528Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei199 – 1991N6-succinyllysine1 Publication
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei252 – 2521N6-succinyllysine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP10518.
    PaxDbiP10518.
    PRIDEiP10518.

    2D gel databases

    REPRODUCTION-2DPAGEP10518.
    SWISS-2DPAGEP10518.

    PTM databases

    PhosphoSiteiP10518.

    Expressioni

    Gene expression databases

    ArrayExpressiP10518.
    BgeeiP10518.
    CleanExiMM_ALAD.
    GenevestigatoriP10518.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP10518. 5 interactions.
    MINTiMINT-1869777.

    Structurei

    Secondary structure

    1
    330
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 103
    Helixi14 – 207
    Helixi28 – 303
    Beta strandi31 – 4212
    Beta strandi44 – 463
    Beta strandi48 – 503
    Beta strandi54 – 574
    Helixi58 – 603
    Helixi61 – 644
    Helixi66 – 694
    Turni70 – 723
    Beta strandi75 – 817
    Helixi100 – 11112
    Beta strandi113 – 1197
    Helixi144 – 16017
    Beta strandi163 – 1653
    Helixi174 – 18310
    Turni185 – 1884
    Beta strandi192 – 1943
    Helixi206 – 2116
    Helixi231 – 24111
    Helixi242 – 2443
    Beta strandi247 – 2548
    Helixi255 – 2573
    Helixi258 – 26710
    Beta strandi273 – 2764
    Helixi279 – 29012
    Helixi296 – 30914
    Beta strandi313 – 3164
    Helixi320 – 3267

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z0IX-ray3.20A/B1-330[»]
    2Z1BX-ray3.30A/B/C/D1-330[»]
    ProteinModelPortaliP10518.
    SMRiP10518. Positions 5-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10518.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Phylogenomic databases

    eggNOGiCOG0113.
    GeneTreeiENSGT00390000006998.
    HOGENOMiHOG000020323.
    HOVERGENiHBG001222.
    InParanoidiP10518.
    KOiK01698.
    OMAiSGYFHPT.
    OrthoDBiEOG751NFP.
    PhylomeDBiP10518.
    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.

    P10518-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHHQSVLHSG YFHPLLRSWQ TAASTVSASN LIYPIFVTDV PDDVQPIASL    50
    PGVARYGVNQ LEEMLRPLVE AGLRCVLIFG VPSRVPKDEQ GSAADSEDSP 100
    TIEAVRLLRK TFPSLLVACD VCLCPYTSHG HCGLLSENGA FLAEESRQRL 150
    AEVALAYAKA GCQVVAPSDM MDGRVEAIKA ALLKHGLGNR VSVMSYSAKF 200
    ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVAR DIQEGADMLM 250
    VKPGLPYLDM VREVKDKHPE LPLAVYQVSG EFAMLWHGAQ AGAFDLRTAV 300
    LETMTAFRRA GADIIITYFA PQLLKWLKEE 330
    Length:330
    Mass (Da):36,024
    Last modified:July 1, 1989 - v1
    Checksum:i84052DC911C153EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13752 mRNA. Translation: CAA32015.1.
    AK032908 mRNA. Translation: BAC28080.1.
    AK167673 mRNA. Translation: BAE39722.1.
    AK168119 mRNA. Translation: BAE40090.1.
    AK168132 mRNA. Translation: BAE40101.1.
    BC055930 mRNA. Translation: AAH55930.1.
    CCDSiCCDS18243.1.
    PIRiS03187.
    RefSeqiNP_001263375.1. NM_001276446.1.
    NP_032551.3. NM_008525.4.
    XP_006537702.1. XM_006537639.1.
    UniGeneiMm.6988.

    Genome annotation databases

    EnsembliENSMUST00000030090; ENSMUSP00000030090; ENSMUSG00000028393.
    ENSMUST00000107444; ENSMUSP00000103068; ENSMUSG00000028393.
    GeneIDi17025.
    KEGGimmu:17025.
    UCSCiuc008tez.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13752 mRNA. Translation: CAA32015.1 .
    AK032908 mRNA. Translation: BAC28080.1 .
    AK167673 mRNA. Translation: BAE39722.1 .
    AK168119 mRNA. Translation: BAE40090.1 .
    AK168132 mRNA. Translation: BAE40101.1 .
    BC055930 mRNA. Translation: AAH55930.1 .
    CCDSi CCDS18243.1.
    PIRi S03187.
    RefSeqi NP_001263375.1. NM_001276446.1.
    NP_032551.3. NM_008525.4.
    XP_006537702.1. XM_006537639.1.
    UniGenei Mm.6988.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Z0I X-ray 3.20 A/B 1-330 [» ]
    2Z1B X-ray 3.30 A/B/C/D 1-330 [» ]
    ProteinModelPortali P10518.
    SMRi P10518. Positions 5-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P10518. 5 interactions.
    MINTi MINT-1869777.

    PTM databases

    PhosphoSitei P10518.

    2D gel databases

    REPRODUCTION-2DPAGE P10518.
    SWISS-2DPAGE P10518.

    Proteomic databases

    MaxQBi P10518.
    PaxDbi P10518.
    PRIDEi P10518.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030090 ; ENSMUSP00000030090 ; ENSMUSG00000028393 .
    ENSMUST00000107444 ; ENSMUSP00000103068 ; ENSMUSG00000028393 .
    GeneIDi 17025.
    KEGGi mmu:17025.
    UCSCi uc008tez.1. mouse.

    Organism-specific databases

    CTDi 210.
    MGIi MGI:96853. Alad.

    Phylogenomic databases

    eggNOGi COG0113.
    GeneTreei ENSGT00390000006998.
    HOGENOMi HOG000020323.
    HOVERGENi HBG001222.
    InParanoidi P10518.
    KOi K01698.
    OMAi SGYFHPT.
    OrthoDBi EOG751NFP.
    PhylomeDBi P10518.
    TreeFami TF300665.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00318 .
    Reactomei REACT_203298. Heme biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei P10518.
    NextBioi 291138.
    PROi P10518.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10518.
    Bgeei P10518.
    CleanExi MM_ALAD.
    Genevestigatori P10518.

    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. "Cloning and sequence of mouse erythroid delta-aminolevulinate dehydratase cDNA."
      Bishop T.R., Hodes Z.I., Frelin L.P., Boyer S.H.
      Nucleic Acids Res. 17:1775-1775(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c, C57BL/6J and DBA/2.
      Tissue: Placenta.
    3. "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].
      Strain: FVB/N.
      Tissue: Colon.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Crystal structure of 5-aminolevulinic acid dehydratase (ALAD) from Mus musculus."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).

    Entry informationi

    Entry nameiHEM2_MOUSE
    AccessioniPrimary (citable) accession number: P10518
    Secondary accession number(s): Q3THV6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 128 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

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3