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

Q2G1J2 (HDOX2_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 55. 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) 2

EC=1.14.99.48
Alternative name(s):
Heme oxygenase 2
Heme-degrading monooxygenase 2
Iron-regulated surface determinant 2
Iron-responsive surface determinant 2
Gene names
Name:isdI
Ordered Locus Names:SAOUHSC_00130
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length108 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. Ref.2

Protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O. Ref.2

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01272

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_01272.

Induction

Transcriptionally regulated by iron and the ferric uptake repressor (fur) protein Probable. 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
Reference 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 – 108108Heme oxygenase (staphylobilin-producing) 2 HAMAP-Rule MF_01272
PRO_0000270094

Regions

Region21 – 288Heme binding By similarity

Sites

Metal binding61Iron By similarity
Metal binding761Iron (heme axial ligand) By similarity
Site661Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2G1J2 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 8AF2718571451004

FASTA10812,791
        10         20         30         40         50         60 
MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE VKILTIWESE 

        70         80         90        100 
DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK 

« Hide

References

« Hide 'large scale' references
[1]"The Staphylococcus aureus NCTC 8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
(In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.
[2]"IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus."
Skaar E.P., Gaspar A.H., Schneewind O.
J. Biol. Chem. 279:436-443(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000253 Genomic DNA. Translation: ABD29311.1.
RefSeqYP_498730.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2G1J2.
SMRQ2G1J2. Positions 1-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_00130.

Proteomic databases

PRIDEQ2G1J2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD29311; ABD29311; SAOUHSC_00130.
GeneID3919839.
KEGGsao:SAOUHSC_00130.
PATRIC19577892. VBIStaAur99865_0122.

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
OMAFRESHSH.
OrthoDBEOG6GTZMS.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-124-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 nameHDOX2_STAA8
AccessionPrimary (citable) accession number: Q2G1J2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 55 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