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P71119

- HMUO_CORDI

UniProt

P71119 - HMUO_CORDI

Protein

Heme oxygenase

Gene

hmuO

Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (28 Nov 2003)
      Previous versions | rss
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    Functioni

    Allows the bacteria to use the host heme as an iron source. Involved in the oxidation of heme and subsequent release of iron from the heme moiety.

    Catalytic activityi

    Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi20 – 201Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. heme oxygenase (decyclizing) activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. heme oxidation Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heme oxygenase (EC:1.14.99.3)
    Gene namesi
    Name:hmuO
    Ordered Locus Names:DIP1669
    OrganismiCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
    Taxonomic identifieri257309 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000002198: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215Heme oxygenasePRO_0000209703Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi257309.DIP1669.

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2417
    Helixi27 – 337
    Helixi39 – 6628
    Turni70 – 723
    Helixi75 – 773
    Helixi80 – 9112
    Beta strandi92 – 943
    Helixi96 – 994
    Helixi104 – 11916
    Helixi122 – 15130
    Helixi155 – 1573
    Helixi159 – 1624
    Helixi169 – 18214
    Helixi187 – 21226

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IW0X-ray1.40A/B/C1-215[»]
    1IW1X-ray1.50A/B/C1-215[»]
    1V8XX-ray1.85A/B/C1-215[»]
    1WNVX-ray1.85A/B/C1-215[»]
    1WNWX-ray1.70A/B/C1-215[»]
    1WNXX-ray1.85A/B1-215[»]
    1WZDX-ray1.35A/B1-215[»]
    1WZFX-ray1.85A/B1-215[»]
    1WZGX-ray1.75A/B1-215[»]
    ProteinModelPortaliP71119.
    SMRiP71119. Positions 2-213.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP71119.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heme oxygenase family.Curated

    Phylogenomic databases

    eggNOGiCOG5398.
    HOGENOMiHOG000233221.
    KOiK00510.
    OMAiEISAHEP.
    OrthoDBiEOG69PQ2G.

    Family and domain databases

    Gene3Di1.20.910.10. 1 hit.
    InterProiIPR002051. Haem_Oase.
    IPR016053. Haem_Oase-like.
    IPR016084. Haem_Oase-like_multi-hlx.
    IPR018207. Haem_oxygenase_CS.
    [Graphical view]
    PANTHERiPTHR10720. PTHR10720. 1 hit.
    PfamiPF01126. Heme_oxygenase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000343. Haem_Oase. 1 hit.
    PRINTSiPR00088. HAEMOXYGNASE.
    SUPFAMiSSF48613. SSF48613. 1 hit.
    PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P71119-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTATAGLAV ELKQSTAQAH EKAEHSTFMS DLLEGRLGVA EFTRLQEQAW    50
    LFYTALEQAA DAVRASGFAE SLLDPALNRA EVLARDLDKL NDGSEWRSRI 100
    TASPAVIDYV NRLEEIRDNV DGPALVAHHY VRYLGDLSGG QVIARMMQRH 150
    YGVDPEALGF YHFEGIAKLK VYKDEYREKL NNLELSDEQR ENLLKEATDA 200
    FVFNHQVFAD LGKGL 215
    Length:215
    Mass (Da):24,116
    Last modified:November 28, 2003 - v2
    Checksum:i60D9E8E2ED7ED456
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341E → K in AAC44832. (PubMed:9006041)Curated
    Sequence conflicti60 – 601A → V in AAC44832. (PubMed:9006041)Curated
    Sequence conflicti92 – 932DG → GS in AAC44832. (PubMed:9006041)Curated
    Sequence conflicti192 – 1921N → H in AAC44832. (PubMed:9006041)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73860 Genomic DNA. Translation: AAC44832.1.
    BX248358 Genomic DNA. Translation: CAE50198.1.
    RefSeqiNP_940009.1. NC_002935.2.
    WP_010935240.1. NC_002935.2.

    Genome annotation databases

    EnsemblBacteriaiCAE50198; CAE50198; DIP1669.
    GeneIDi2648714.
    KEGGicdi:DIP1669.
    PATRICi21484548. VBICorDip47633_1650.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73860 Genomic DNA. Translation: AAC44832.1 .
    BX248358 Genomic DNA. Translation: CAE50198.1 .
    RefSeqi NP_940009.1. NC_002935.2.
    WP_010935240.1. NC_002935.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IW0 X-ray 1.40 A/B/C 1-215 [» ]
    1IW1 X-ray 1.50 A/B/C 1-215 [» ]
    1V8X X-ray 1.85 A/B/C 1-215 [» ]
    1WNV X-ray 1.85 A/B/C 1-215 [» ]
    1WNW X-ray 1.70 A/B/C 1-215 [» ]
    1WNX X-ray 1.85 A/B 1-215 [» ]
    1WZD X-ray 1.35 A/B 1-215 [» ]
    1WZF X-ray 1.85 A/B 1-215 [» ]
    1WZG X-ray 1.75 A/B 1-215 [» ]
    ProteinModelPortali P71119.
    SMRi P71119. Positions 2-213.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 257309.DIP1669.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE50198 ; CAE50198 ; DIP1669 .
    GeneIDi 2648714.
    KEGGi cdi:DIP1669.
    PATRICi 21484548. VBICorDip47633_1650.

    Phylogenomic databases

    eggNOGi COG5398.
    HOGENOMi HOG000233221.
    KOi K00510.
    OMAi EISAHEP.
    OrthoDBi EOG69PQ2G.

    Miscellaneous databases

    EvolutionaryTracei P71119.

    Family and domain databases

    Gene3Di 1.20.910.10. 1 hit.
    InterProi IPR002051. Haem_Oase.
    IPR016053. Haem_Oase-like.
    IPR016084. Haem_Oase-like_multi-hlx.
    IPR018207. Haem_oxygenase_CS.
    [Graphical view ]
    PANTHERi PTHR10720. PTHR10720. 1 hit.
    Pfami PF01126. Heme_oxygenase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000343. Haem_Oase. 1 hit.
    PRINTSi PR00088. HAEMOXYGNASE.
    SUPFAMi SSF48613. SSF48613. 1 hit.
    PROSITEi PS00593. HEME_OXYGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin."
      Schmitt M.P.
      J. Bacteriol. 179:838-845(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C7.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

    Entry informationi

    Entry nameiHMUO_CORDI
    AccessioniPrimary (citable) accession number: P71119
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 28, 2003
    Last modified: October 1, 2014
    This is version 97 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, Reference 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