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O28305

- HEM2_ARCFU

UniProt

O28305 - HEM2_ARCFU

Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Jan 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 bindingi120 – 1201Zinc; catalyticBy similarity
    Metal bindingi122 – 1221Zinc; catalyticBy similarity
    Metal bindingi130 – 1301Zinc; catalyticBy similarity
    Active sitei195 – 1951Schiff-base intermediate with substrateBy similarity
    Binding sitei205 – 2051Substrate 1By similarity
    Binding sitei217 – 2171Substrate 1By similarity
    Metal bindingi233 – 2331MagnesiumBy similarity
    Active sitei248 – 2481Schiff-base intermediate with substrateBy similarity
    Binding sitei274 – 2741Substrate 2By similarity
    Binding sitei312 – 3121Substrate 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. porphobilinogen synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciAFUL224325:GJBC-2011-MONOMER.
    UniPathwayiUPA00251; UER00318.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
    Short name:
    ALAD
    Short name:
    ALADH
    Alternative name(s):
    Porphobilinogen synthase
    Gene namesi
    Name:hemB
    Ordered Locus Names:AF_1974
    OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
    Taxonomic identifieri224325 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
    ProteomesiUP000002199: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 322322Delta-aminolevulinic acid dehydratasePRO_0000140522Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer.By similarity

    Protein-protein interaction databases

    STRINGi224325.AF1974.

    Structurei

    3D structure databases

    ProteinModelPortaliO28305.
    SMRiO28305. Positions 6-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Phylogenomic databases

    eggNOGiCOG0113.
    KOiK01698.
    OMAiDMILTYF.

    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.

    O28305-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEFPKVRMR RLRKANLRWM FREARLSPEN LITPIFVDEN IKEKKPIESM    50
    PDYFRIPLEM VDKEVEECLE KDLRSFILFG IPSYKDETGS SAYDQNGVIQ 100
    KAVRRIKAEF PDAVIVTDVC LCEYTTHGHC GVVKDGEIVN DETLPIIGKT 150
    AVSHAESGAD IVAPSGMMDG MVKAIREALD AAGFESTPIM SYSAKYASNF 200
    YSPFRDAAES GFKFGDRRGY QMDIHNAREA MREIELDVKE GADIIMVKPA 250
    LPYLDIIRMV RERFDLPLAA YNVSGEYSMI KAAIKNGWLS EEAIYEVLIS 300
    IKRAGADLII TYHSKEIAEK LQ 322
    Length:322
    Mass (Da):36,398
    Last modified:January 1, 1998 - v1
    Checksum:i5FE684E6B394B509
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89292.1.
    PIRiE69496.
    RefSeqiNP_070798.1. NC_000917.1.

    Genome annotation databases

    EnsemblBacteriaiAAB89292; AAB89292; AF_1974.
    GeneIDi1485196.
    KEGGiafu:AF1974.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89292.1 .
    PIRi E69496.
    RefSeqi NP_070798.1. NC_000917.1.

    3D structure databases

    ProteinModelPortali O28305.
    SMRi O28305. Positions 6-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224325.AF1974.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB89292 ; AAB89292 ; AF_1974 .
    GeneIDi 1485196.
    KEGGi afu:AF1974.

    Phylogenomic databases

    eggNOGi COG0113.
    KOi K01698.
    OMAi DMILTYF.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00318 .
    BioCyci AFUL224325:GJBC-2011-MONOMER.

    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 complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
      Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
      , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
      Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

    Entry informationi

    Entry nameiHEM2_ARCFU
    AccessioniPrimary (citable) accession number: O28305
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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