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P64334

- HEM2_STAAN

UniProt

P64334 - HEM2_STAAN

Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      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 bindingi118 – 1181Zinc; catalyticBy similarity
    Metal bindingi120 – 1201Zinc; catalyticBy similarity
    Metal bindingi128 – 1281Zinc; 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 sitei313 – 3131Substrate 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

    BioCyciSAUR158879:GJCB-1565-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:SA1492
    OrganismiStaphylococcus aureus (strain N315)
    Taxonomic identifieri158879 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000751: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 324324Delta-aminolevulinic acid dehydratasePRO_0000140512Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer.By similarity

    Protein-protein interaction databases

    STRINGi158879.SA1492.

    Structurei

    3D structure databases

    ProteinModelPortaliP64334.
    SMRiP64334. Positions 5-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Phylogenomic databases

    eggNOGiCOG0113.
    HOGENOMiHOG000020323.
    KOiK01698.
    OMAiDMILTYF.
    OrthoDBiEOG6VXFCB.

    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.

    P64334-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFDRHRRLR SSATMRDMVR ENHVRKEDLI YPIFVVEKDD VKKEIKSLPG    50
    VYQISLNLLE SELKEAYDLG IRAIMFFGVP NSKDDIGTGA YIHDGVIQQA 100
    TRIAKKMYDD LLIVADTCLC EYTDHGHCGV IDDHTHDVDN DKSLPLLVKT 150
    AISQVEAGAD IIAPSNMMDG FVAEIRRGLD EAGYYNIPIM SYGVKYASSF 200
    FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE GCDMMIVKPA 250
    LSYLDIVRDV KNHTNVPVVA YNVSGEYSMT KAAAQNGWID EERVVMEQMV 300
    SMKRAGADMI ITYFAKDICR YLDK 324
    Length:324
    Mass (Da):36,583
    Last modified:October 11, 2004 - v1
    Checksum:iBF24378E01E7C93E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42759.1.
    PIRiB89950.
    RefSeqiNP_374780.1. NC_002745.2.

    Genome annotation databases

    EnsemblBacteriaiBAB42759; BAB42759; BAB42759.
    GeneIDi1124337.
    KEGGisau:SA1492.
    PATRICi19575284. VBIStaAur116463_1612.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42759.1 .
    PIRi B89950.
    RefSeqi NP_374780.1. NC_002745.2.

    3D structure databases

    ProteinModelPortali P64334.
    SMRi P64334. Positions 5-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158879.SA1492.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB42759 ; BAB42759 ; BAB42759 .
    GeneIDi 1124337.
    KEGGi sau:SA1492.
    PATRICi 19575284. VBIStaAur116463_1612.

    Phylogenomic databases

    eggNOGi COG0113.
    HOGENOMi HOG000020323.
    KOi K01698.
    OMAi DMILTYF.
    OrthoDBi EOG6VXFCB.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00318 .
    BioCyci SAUR158879:GJCB-1565-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: N315.
    2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
      Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
      Submitted (OCT-2007) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: N315.

    Entry informationi

    Entry nameiHEM2_STAAN
    AccessioniPrimary (citable) accession number: P64334
    Secondary accession number(s): Q99TJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 61 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3