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Q8NX62 (HDOX1_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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 (staphylobilin-producing) 1

EC=1.14.99.48
Alternative name(s):
Heme oxygenase 1
Heme-degrading monooxygenase 1
Iron-regulated surface determinant 1
Iron-responsive surface determinant 1
Gene names
Name:isdG
Ordered Locus Names:MW1018
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length107 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Ref.2

Catalytic activity

Protoheme + 4 AH2 + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O. HAMAP-Rule MF_01272

Protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O. HAMAP-Rule MF_01272

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01272.

Miscellaneous

IsdG 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.

Sequence similarities

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processheme catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron assimilation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheme binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

heme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 107107Heme oxygenase (staphylobilin-producing) 1 HAMAP-Rule MF_01272
PRO_0000270089

Regions

Region22 – 298Heme binding By similarity

Sites

Metal binding71Iron By similarity
Metal binding771Iron (heme axial ligand) By similarity
Site671Transition state stabilizer By similarity

Experimental info

Mutagenesis71N → A: Loss of activity. Ref.2
Mutagenesis171K → A: No effect. Ref.2
Mutagenesis231F → A: No effect. Ref.2
Mutagenesis381M → A: Slight loss of activity. Changes in heme binding. Ref.2
Mutagenesis671W → A: Loss of activity. Ref.2
Mutagenesis701S → A: No effect. Ref.2
Mutagenesis771H → A: Loss of activity. Ref.2

Secondary structure

................ 107
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8NX62 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: DB13A134D5EC4FF0

FASTA10712,546
        10         20         30         40         50         60 
MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS 

        70         80         90        100 
KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK 

« Hide

References

« Hide 'large scale' references
[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.
[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 (1.9 ANGSTROMS), FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-7; LYS-17; PHE-23; MET-38; TRP-67; SER-70 AND HIS-77.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000033 Genomic DNA. Translation: BAB94883.1.
RefSeqNP_645835.1. NC_003923.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XBWX-ray1.90A/B/C/D1-107[»]
ProteinModelPortalQ8NX62.
SMRQ8NX62. Positions 1-107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196620.MW1018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB94883; BAB94883; BAB94883.
GeneID1003130.
KEGGsam:MW1018.
PATRIC19568616. VBIStaAur44266_1067.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
OMAVRHQSQD.
OrthoDBEOG6GTZMS.

Enzyme and pathway databases

BioCycSAUR196620:GJ9Z-1042-MONOMER.

Family and domain databases

HAMAPMF_01272. Heme_degrading_monooxygenase.
InterProIPR007138. Antibiotic_mOase.
IPR011008. Dimeric_a/b-barrel.
IPR023953. Heme-degrad_mOase.
[Graphical view]
PfamPF03992. ABM. 1 hit.
[Graphical view]
SUPFAMSSF54909. SSF54909. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8NX62.

Entry information

Entry nameHDOX1_STAAW
AccessionPrimary (citable) accession number: Q8NX62
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 75 of the entry and version 1 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