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P71119 (HMUO_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heme oxygenase

EC=1.14.99.3
Gene names
Name:hmuO
Ordered Locus Names:DIP1669
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processheme oxidation

Inferred from electronic annotation. Source: InterPro

   Molecular_functionheme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Heme oxygenase
PRO_0000209703

Sites

Metal binding201Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict341E → K in AAC44832. Ref.1
Sequence conflict601A → V in AAC44832. Ref.1
Sequence conflict92 – 932DG → GS in AAC44832. Ref.1
Sequence conflict1921N → H in AAC44832. Ref.1

Secondary structure

............................ 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P71119 [UniParc].

Last modified November 28, 2003. Version 2.
Checksum: 60D9E8E2ED7ED456

FASTA21524,116
        10         20         30         40         50         60 
MTTATAGLAV ELKQSTAQAH EKAEHSTFMS DLLEGRLGVA EFTRLQEQAW LFYTALEQAA 

        70         80         90        100        110        120 
DAVRASGFAE SLLDPALNRA EVLARDLDKL NDGSEWRSRI TASPAVIDYV NRLEEIRDNV 

       130        140        150        160        170        180 
DGPALVAHHY VRYLGDLSGG QVIARMMQRH YGVDPEALGF YHFEGIAKLK VYKDEYREKL 

       190        200        210 
NNLELSDEQR ENLLKEATDA FVFNHQVFAD LGKGL 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129."
Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S. expand/collapse author list , Quail M.A., Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., Parkhill J.
Nucleic Acids Res. 31:6516-6523(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73860 Genomic DNA. Translation: AAC44832.1.
BX248358 Genomic DNA. Translation: CAE50198.1.
RefSeqNP_940009.1. NC_002935.2.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP71119.
SMRP71119. Positions 2-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP1669.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE50198; CAE50198; DIP1669.
GeneID2648714.
KEGGcdi:DIP1669.
PATRIC21484548. VBICorDip47633_1650.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG5398.
HOGENOMHOG000233221.
KOK00510.
OMAYAPLYFP.
OrthoDBEOG69PQ2G.
ProtClustDBCLSK900077.

Family and domain databases

Gene3D1.20.910.10. 1 hit.
InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERPTHR10720. PTHR10720. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
SUPFAMSSF48613. SSF48613. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP71119.

Entry information

Entry nameHMUO_CORDI
AccessionPrimary (citable) accession number: P71119
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 28, 2003
Last modified: November 13, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references