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Q7A827

- HDOX2_STAAN

UniProt

Q7A827 - HDOX2_STAAN

Protein

Heme oxygenase (staphylobilin-producing) 2

Gene

isdI

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 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.2 PublicationsUniRule annotation

    Catalytic activityi

    Protoheme + 4 AH2 + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.1 PublicationUniRule annotation
    Protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.1 PublicationUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi6 – 61Iron
    Sitei66 – 661Transition state stabilizer
    Metal bindingi76 – 761Iron (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-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:SA0160
    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
    Mutagenesisi66 – 661W → A: Inactive. 1 Publication
    Mutagenesisi66 – 661W → F: Heme degradation activity is approximately half that of the wild-type enzyme. 1 Publication
    Mutagenesisi66 – 661W → L: Inactive. 1 Publication
    Mutagenesisi66 – 661W → Y: Heme degradation activity is approximately half that of the wild-type enzyme. Heme binds to this enzyme with less heme ruffling than observed for wild-type. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 108108Heme oxygenase (staphylobilin-producing) 2PRO_0000270092Add
    BLAST

    Proteomic databases

    PRIDEiQ7A827.

    Interactioni

    Subunit structurei

    Homodimer.4 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi158879.SA0160.

    Structurei

    Secondary structure

    1
    108
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 109
    Helixi15 – 206
    Helixi21 – 233
    Helixi28 – 303
    Beta strandi34 – 429
    Beta strandi47 – 5812
    Helixi60 – 678
    Helixi70 – 756
    Turni76 – 783
    Beta strandi92 – 10716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZDPX-ray1.50A/B1-108[»]
    3LGMX-ray1.88A/B1-108[»]
    3LGNX-ray1.50A/B1-108[»]
    3QGPX-ray1.80A/B1-108[»]
    4FNHX-ray1.90A/B1-108[»]
    4FNIX-ray1.80A/B1-108[»]
    ProteinModelPortaliQ7A827.
    SMRiQ7A827. Positions 1-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7A827.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 288Heme 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.
    KOiK07145.
    OMAiGICKTTH.
    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.

    Q7A827-1 [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:July 5, 2004 - v1
    Checksum:i8AF2718571451004
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB41380.1.
    PIRiA89778.
    RefSeqiNP_373402.1. NC_002745.2.

    Genome annotation databases

    EnsemblBacteriaiBAB41380; BAB41380; BAB41380.
    GeneIDi1122935.
    KEGGisau:SA0160.
    PATRICi19572351. VBIStaAur116463_0165.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB41380.1 .
    PIRi A89778.
    RefSeqi NP_373402.1. NC_002745.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZDP X-ray 1.50 A/B 1-108 [» ]
    3LGM X-ray 1.88 A/B 1-108 [» ]
    3LGN X-ray 1.50 A/B 1-108 [» ]
    3QGP X-ray 1.80 A/B 1-108 [» ]
    4FNH X-ray 1.90 A/B 1-108 [» ]
    4FNI X-ray 1.80 A/B 1-108 [» ]
    ProteinModelPortali Q7A827.
    SMRi Q7A827. Positions 1-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158879.SA0160.

    Proteomic databases

    PRIDEi Q7A827.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB41380 ; BAB41380 ; BAB41380 .
    GeneIDi 1122935.
    KEGGi sau:SA0160.
    PATRICi 19572351. VBIStaAur116463_0165.

    Phylogenomic databases

    eggNOGi COG2329.
    HOGENOMi HOG000008026.
    KOi K07145.
    OMAi GICKTTH.
    OrthoDBi EOG6GTZMS.

    Enzyme and pathway databases

    BioCyci SAUR158879:GJCB-165-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q7A827.

    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. "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.
    3. "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 (1.50 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME, FUNCTION, SUBUNIT.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    5. "Heme ruffling enables the catalytic activity of the heme degrading enzyme IsdI."
      Takayama S.J., Ukpabi G.N., Murphy M.E.P., Mauk A.G.
      Submitted (JAN-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME, SUBUNIT.
    6. "Inactivation of the heme degrading enzyme IsdI by an active site substitution that diminishes heme ruffling."
      Ukpabi G., Takayama S.J., Mauk A.G., Murphy M.E.
      J. Biol. Chem. 287:34179-34188(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-108 OF MUTANT THR-66 IN COMPLEX WITH HEME, MUTAGENESIS OF TRP-66, SUBUNIT.

    Entry informationi

    Entry nameiHDOX2_STAAN
    AccessioniPrimary (citable) accession number: Q7A827
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 74 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

    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