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Q7A827 (HDOX2_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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) 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:SA0160
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [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. Ref.3 Ref.4

Catalytic activity

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

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

Subunit structure

Homodimer. Ref.3 Ref.4 Ref.5 Ref.6

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 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 – 108108Heme oxygenase (staphylobilin-producing) 2 HAMAP-Rule MF_01272
PRO_0000270092

Regions

Region21 – 288Heme binding HAMAP-Rule MF_01272

Sites

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

Experimental info

Mutagenesis661W → A: Inactive. Ref.6
Mutagenesis661W → F: Heme degradation activity is approximately half that of the wild-type enzyme. Ref.6
Mutagenesis661W → L: Inactive. Ref.6
Mutagenesis661W → Y: Heme degradation activity is approximately half that of the wild-type enzyme. Heme binds to this enzyme with less heme ruffling than observed for wild-type. Ref.6

Secondary structure

................... 108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7A827 [UniParc].

Last modified July 5, 2004. 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]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.
[3]"Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus."
Lee W.C., Reniere M.L., Skaar E.P., Murphy M.E.
J. Biol. Chem. 283:30957-30963(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME, FUNCTION, SUBUNIT.
[4]"The IsdG-family of haem oxygenases degrades haem to a novel chromophore."
Reniere M.L., Ukpabi G.N., Harry S.R., Stec D.F., Krull R., Wright D.W., Bachmann B.O., Murphy M.E., Skaar E.P.
Mol. Microbiol. 75:1529-1538(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[5]"Heme ruffling enables the catalytic activity of the heme degrading enzyme IsdI."
Takayama S.J., Ukpabi G.N., Murphy M.E.P., Mauk A.G.
Submitted (JAN-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME, SUBUNIT.
[6]"Inactivation of the heme degrading enzyme IsdI by an active site substitution that diminishes heme ruffling."
Ukpabi G., Takayama S.J., Mauk A.G., Murphy M.E.
J. Biol. Chem. 287:34179-34188(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-108 OF MUTANT THR-66 IN COMPLEX WITH HEME, MUTAGENESIS OF TRP-66, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB41380.1.
PIRA89778.
RefSeqNP_373402.1. NC_002745.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZDPX-ray1.50A/B1-108[»]
3LGMX-ray1.88A/B1-108[»]
3LGNX-ray1.50A/B1-108[»]
3QGPX-ray1.80A/B1-108[»]
4FNHX-ray1.90A/B1-108[»]
4FNIX-ray1.80A/B1-108[»]
ProteinModelPortalQ7A827.
SMRQ7A827. Positions 1-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158879.SA0160.

Proteomic databases

PRIDEQ7A827.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB41380; BAB41380; BAB41380.
GeneID1122935.
KEGGsau:SA0160.
PATRIC19572351. VBIStaAur116463_0165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
OMAGICKTTH.
OrthoDBEOG6GTZMS.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-165-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

EvolutionaryTraceQ7A827.

Entry information

Entry nameHDOX2_STAAN
AccessionPrimary (citable) accession number: Q7A827
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 72 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