Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2FHU5 (HDOX1_STAA3) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:SAUSA300_1035
OrganismStaphylococcus aureus (strain USA300) [Complete proteome] [HAMAP]
Taxonomic identifier367830 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length107 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP-Rule MF_01272

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 By similarity. HAMAP-Rule MF_01272

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01272.

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 termComplete 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_0000270095

Regions

Region22 – 298Heme binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q2FHU5 [UniParc].

Last modified March 21, 2006. 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

[1]"Complete genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus."
Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., Perdreau-Remington F.
Lancet 367:731-739(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USA300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000255 Genomic DNA. Translation: ABD22802.1.
RefSeqYP_493733.1. NC_007793.1.

3D structure databases

ProteinModelPortalQ2FHU5.
SMRQ2FHU5. Positions 1-107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING451515.SAUSA300_1035.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD22802; ABD22802; SAUSA300_1035.
GeneID3913448.
KEGGsaa:SAUSA300_1035.
PATRIC19591409. VBIStaAur129981_1133.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
OMAGEGERIM.
OrthoDBEOG6GTZMS.
ProtClustDBPRK13312.

Enzyme and pathway databases

BioCycSAUR451515:GH3C-1035-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...

Entry information

Entry nameHDOX1_STAA3
AccessionPrimary (citable) accession number: Q2FHU5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: March 21, 2006
Last modified: March 19, 2014
This is version 57 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