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Q7A827 (ISDI_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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-degrading monooxygenase isdI

EC=1.14.99.3
Alternative name(s):
Heme oxygenase
Iron-regulated surface determinant isdI
Iron-responsive surface determinant isdI
Gene names
Name:isdI
Ordered Locus Names:SA0160
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

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 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 MF_01272

Catalytic activity

Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. HAMAP MF_01272

Subunit structure

Homodimer By similarity. HAMAP MF_01272

Subcellular location

Cytoplasm By similarity HAMAP 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 processiron assimilation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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-degrading monooxygenase isdI HAMAP MF_01272
PRO_0000270092

Sites

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

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

[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: 11418146] [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.
+Additional computationally mapped references.

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[»]
ProteinModelPortalQ7A827.
SMRQ7A827. Positions 1-108.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7A827.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000001858; EBSTAP00000001858; EBSTAG00000001858.
GeneID1122935.
GenomeReviewsGene locus SA0160 in contig BA000018_GR.
KEGGsau:SA0160.
PATRIC19572351. VBIStaAur116463_0165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2329.
GeneTreeEBGT00050000024362.
HOGENOMHBG616589.
OMAWTKSSAF.
ProtClustDBPRK13313.

Enzyme and pathway databases

BioCycSAUR158879:SA0160-MONOMER.

Family and domain databases

HAMAPMF_01272. IsdG.
[Tree]
InterProIPR007138. Antibiotic_mOase.
IPR011008. Dimeric_a/b-barrel.
IPR023953. Heme-degrad_mOase.
[Graphical view]
KOK07145.
PfamPF03992. ABM. 1 hit.
[Graphical view]
SUPFAMSSF54909. Dimer_A_B_barrel. 1 hit.
ProtoNetSearch...

Entry information

Entry nameISDI_STAAN
AccessionPrimary (citable) accession number: Q7A827
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 5, 2004
Last modified: January 25, 2012
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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families