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Q7A649

- HDOX1_STAAN

UniProt

Q7A649 - HDOX1_STAAN

Protein

Heme oxygenase (staphylobilin-producing) 1

Gene

isdG

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 5 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 staphylobilins (a mixture of 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.1 Publication

    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 bindingi7 – 71Iron
    Sitei67 – 671Transition state stabilizerUniRule annotation
    Metal bindingi77 – 771Iron (heme axial ligand)

    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

    BioCyciSAUR158879:GJCB-1039-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heme oxygenase (staphylobilin-producing) 1UniRule annotation (EC:1.14.99.48UniRule annotation)
    Alternative name(s):
    Heme oxygenase 1UniRule annotation
    Heme-degrading monooxygenase 1UniRule annotation
    Iron-regulated surface determinant 1UniRule annotation
    Iron-responsive surface determinant 1UniRule annotation
    Gene namesi
    Name:isdGUniRule annotation
    Ordered Locus Names:SA0983
    OrganismiStaphylococcus aureus (strain N315)
    Taxonomic identifieri158879 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000751: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71N → A: Absence of oxygenase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 107107Heme oxygenase (staphylobilin-producing) 1PRO_0000270091Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi158879.SA0983.

    Structurei

    Secondary structure

    1
    107
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1210
    Helixi16 – 227
    Helixi29 – 313
    Beta strandi35 – 439
    Beta strandi47 – 5913
    Helixi61 – 688
    Helixi71 – 777
    Turni83 – 853
    Beta strandi91 – 10616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZDOX-ray1.80A/B/C/D1-107[»]
    ProteinModelPortaliQ7A649.
    SMRiQ7A649. Positions 1-107.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7A649.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 9290ABMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 298Heme binding

    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.
    OrthoDBiEOG6GTZMS.

    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.

    Q7A649-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD    50
    EVKILTVWKS KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD 100
    IGYSYMK 107
    Length:107
    Mass (Da):12,546
    Last modified:January 9, 2007 - v2
    Checksum:iDB13A134D5EC4FF0
    GO

    Sequence cautioni

    The sequence BAB42232.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42232.1. Different initiation.
    PIRiD89884.

    Genome annotation databases

    EnsemblBacteriaiBAB42232; BAB42232; BAB42232.
    PATRICi19574162. VBIStaAur116463_1051.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42232.1 . Different initiation.
    PIRi D89884.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZDO X-ray 1.80 A/B/C/D 1-107 [» ]
    ProteinModelPortali Q7A649.
    SMRi Q7A649. Positions 1-107.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158879.SA0983.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB42232 ; BAB42232 ; BAB42232 .
    PATRICi 19574162. VBIStaAur116463_1051.

    Phylogenomic databases

    eggNOGi COG2329.
    HOGENOMi HOG000008026.
    OrthoDBi EOG6GTZMS.

    Enzyme and pathway databases

    BioCyci SAUR158879:GJCB-1039-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q7A649.

    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: N315.
    2. "Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus."
      Lee W.C., Reniere M.L., Skaar E.P., Murphy M.E.
      J. Biol. Chem. 283:30957-30963(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-7 IN COMPLEX WITH HEME, FUNCTION, MUTAGENESIS OF ASN-7, SUBUNIT.

    Entry informationi

    Entry nameiHDOX1_STAAN
    AccessioniPrimary (citable) accession number: Q7A649
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 70 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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