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O42768

- HEM2_CANGA

UniProt

O42768 - HEM2_CANGA

Protein

Delta-aminolevulinic acid dehydratase

Gene

HEM2

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      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 1 zinc ion per monomer.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi133 – 1331Zinc; catalyticBy similarity
    Metal bindingi135 – 1351Zinc; catalyticBy similarity
    Metal bindingi143 – 1431Zinc; catalyticBy similarity
    Active sitei210 – 2101Schiff-base intermediate with substrateBy similarity
    Binding sitei220 – 2201Substrate 1By similarity
    Binding sitei232 – 2321Substrate 1By similarity
    Active sitei263 – 2631Schiff-base intermediate with substrateBy similarity
    Binding sitei290 – 2901Substrate 2By similarity
    Binding sitei329 – 3291Substrate 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:HEM2
    Ordered Locus Names:CAGL0D06138g
    OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
    Taxonomic identifieri284593 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces
    ProteomesiUP000002428: Chromosome D

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 340340Delta-aminolevulinic acid dehydratasePRO_0000140532Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO42768.
    SMRiO42768. Positions 1-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Phylogenomic databases

    HOGENOMiHOG000020323.
    KOiK01698.
    OMAiVSRAMSY.
    OrthoDBiEOG779P7W.

    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.

    O42768-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHTADFLDIE PTEISSILSG GYNHPLLREW QSERQLKKNM LIFPLFISDI    50
    PDEATPIDSL PNIKRFGINK LVDYVKPLVE KGLRSVILFG VPLKEGTKDP 100
    VGTAADDPEG PVIQAIKLLR KEFPELYIIC DVCLCEYTSH GHCGVLYDDG 150
    TINRERSVSR IAAVAVNYAK AGAHCVAPSD MIDGRIKDIK KGLISAGLAH 200
    KTFVLSYAAK FSGNLYGPFR DAACSSPSNG DRKCYQLPQA GRGLARRALA 250
    RDKNEGADGI IVKPSTFYLD IMRDASEICE DLPICAYHVS GEYAMLHAAA 300
    EKGIVDLKSI AFESHEGFLR AGARLIISYF TPEFLDWLSN 340
    Length:340
    Mass (Da):37,425
    Last modified:June 1, 1998 - v1
    Checksum:iE5819CE183FF83E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038566 Genomic DNA. Translation: AAB94926.1.
    CR380950 Genomic DNA. Translation: CAG58584.1.
    RefSeqiXP_445673.1. XM_445673.1.

    Genome annotation databases

    GeneIDi2887248.
    KEGGicgr:CAGL0D06138g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038566 Genomic DNA. Translation: AAB94926.1 .
    CR380950 Genomic DNA. Translation: CAG58584.1 .
    RefSeqi XP_445673.1. XM_445673.1.

    3D structure databases

    ProteinModelPortali O42768.
    SMRi O42768. Positions 1-338.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2887248.
    KEGGi cgr:CAGL0D06138g.

    Phylogenomic databases

    HOGENOMi HOG000020323.
    KOi K01698.
    OMAi VSRAMSY.
    OrthoDBi EOG779P7W.

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 2001-L5.
    2. "Genome evolution in yeasts."
      Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
      , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

    Entry informationi

    Entry nameiHEM2_CANGA
    AccessioniPrimary (citable) accession number: O42768
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    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