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Q99X56

- HDOX2_STAAM

UniProt

Q99X56 - HDOX2_STAAM

Protein

Heme oxygenase (staphylobilin-producing) 2

Gene

isdI

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the oxo-bilirubin chromophore staphylobilin (a mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin) in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.UniRule annotation

    Catalytic activityi

    Protoheme + 4 AH2 + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.UniRule annotation
    Protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi6 – 61IronUniRule annotation
    Sitei66 – 661Transition state stabilizerUniRule annotation
    Metal bindingi76 – 761Iron (heme axial ligand)UniRule annotation

    GO - Molecular functioni

    1. heme binding Source: UniProtKB-HAMAP
    2. heme oxygenase (decyclizing) activity Source: UniProtKB-HAMAP
    3. iron ion binding Source: UniProtKB-HAMAP
    4. monooxygenase activity Source: UniProtKB-KW

    GO - Biological processi

    1. heme catabolic process Source: UniProtKB-HAMAP
    2. iron assimilation Source: InterPro

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciSAUR158878:GJJ5-165-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heme oxygenase (staphylobilin-producing) 2UniRule annotation (EC:1.14.99.48UniRule annotation)
    Alternative name(s):
    Heme oxygenase 2UniRule annotation
    Heme-degrading monooxygenase 2UniRule annotation
    Iron-regulated surface determinant 2UniRule annotation
    Iron-responsive surface determinant 2UniRule annotation
    Gene namesi
    Name:isdI
    Ordered Locus Names:SAV0165
    OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
    Taxonomic identifieri158878 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000002481: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 108108Heme oxygenase (staphylobilin-producing) 2PRO_0000270088Add
    BLAST

    Proteomic databases

    PRIDEiQ99X56.

    Interactioni

    Subunit structurei

    Homodimer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi158878.SAV0165.

    Structurei

    Secondary structure

    1
    108
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 109
    Helixi15 – 184
    Helixi19 – 235
    Helixi28 – 303
    Beta strandi34 – 429
    Beta strandi46 – 5813
    Helixi60 – 678
    Helixi70 – 745
    Beta strandi91 – 10717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SQEX-ray1.50A/B1-108[»]
    ProteinModelPortaliQ99X56.
    SMRiQ99X56. Positions 1-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99X56.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 9392ABMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 288Heme bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.UniRule annotation
    Contains 1 ABM domain.Curated

    Phylogenomic databases

    eggNOGiCOG2329.
    HOGENOMiHOG000008026.
    KOiK07145.
    OMAiFRESHSH.
    OrthoDBiEOG6GTZMS.
    PhylomeDBiQ99X56.

    Family and domain databases

    HAMAPiMF_01272. Heme_degrading_monooxygenase.
    InterProiIPR007138. ABM-like.
    IPR011008. Dimeric_a/b-barrel.
    IPR023953. IsdG.
    [Graphical view]
    PfamiPF03992. ABM. 1 hit.
    [Graphical view]
    SUPFAMiSSF54909. SSF54909. 1 hit.
    PROSITEiPS51725. ABM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99X56-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE    50
    VKILTIWESE DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY 100
    DIGYHYQK 108
    Length:108
    Mass (Da):12,791
    Last modified:June 1, 2001 - v1
    Checksum:i8AF2718571451004
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB56327.1.
    RefSeqiNP_370689.1. NC_002758.2.

    Genome annotation databases

    EnsemblBacteriaiBAB56327; BAB56327; SAV0165.
    GeneIDi1120124.
    KEGGisav:SAV0165.
    PATRICi19560931. VBIStaAur52173_0163.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB56327.1 .
    RefSeqi NP_370689.1. NC_002758.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SQE X-ray 1.50 A/B 1-108 [» ]
    ProteinModelPortali Q99X56.
    SMRi Q99X56. Positions 1-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158878.SAV0165.

    Proteomic databases

    PRIDEi Q99X56.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB56327 ; BAB56327 ; SAV0165 .
    GeneIDi 1120124.
    KEGGi sav:SAV0165.
    PATRICi 19560931. VBIStaAur52173_0163.

    Phylogenomic databases

    eggNOGi COG2329.
    HOGENOMi HOG000008026.
    KOi K07145.
    OMAi FRESHSH.
    OrthoDBi EOG6GTZMS.
    PhylomeDBi Q99X56.

    Enzyme and pathway databases

    BioCyci SAUR158878:GJJ5-165-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q99X56.

    Family and domain databases

    HAMAPi MF_01272. Heme_degrading_monooxygenase.
    InterProi IPR007138. ABM-like.
    IPR011008. Dimeric_a/b-barrel.
    IPR023953. IsdG.
    [Graphical view ]
    Pfami PF03992. ABM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54909. SSF54909. 1 hit.
    PROSITEi PS51725. ABM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Mu50 / ATCC 700699.
    2. "Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases."
      Wu R., Skaar E.P., Zhang R., Joachimiak G., Gornicki P., Schneewind O., Joachimiak A.
      J. Biol. Chem. 280:2840-2846(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiHDOX2_STAAM
    AccessioniPrimary (citable) accession number: Q99X56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    IsdI seems to carry out oxygenation of the heme without the assistance of any of the prosthetic groups or cofactors normally associated with activation of molecular oxygen.

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3