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Q7A649 (HDOX1_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Heme-degrading monooxygenase 1
EC=1.14.99.-
Alternative name(s):
Heme oxygenase 1
Iron-regulated surface determinant 1
Iron-responsive surface determinant 1
Gene names
Name:isdG
Ordered Locus Names:SA0983
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

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 staphylobilins (a mixture of 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.2

Catalytic activity

Heme + 3 AH2 + 3 O2 = staphylobilins + Fe2+ + CO + 3 A + 3 H2O. HAMAP-Rule MF_01272

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence caution

The sequence BAB42232.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 107107Heme-degrading monooxygenase 1 HAMAP-Rule MF_01272
PRO_0000270091

Regions

Region22 – 298Heme binding HAMAP-Rule MF_01272

Sites

Metal binding71Iron
Metal binding771Iron (heme axial ligand)
Site671Transition state stabilizer Potential

Experimental info

Mutagenesis71N → A: Absence of oxygenase activity. Ref.2

Secondary structure

1 ................... 107
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7A649 [UniParc].

Last modified January 9, 2007. Version 2.
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]"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]"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 (1.8 ANGSTROMS) OF MUTANT ALA-7 IN COMPLEX WITH HEME, FUNCTION, MUTAGENESIS OF ASN-7, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000018 Genomic DNA. Translation: BAB42232.1. Different initiation.
PIRD89884.
RefSeqNP_374253.2. NC_002745.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZDOX-ray1.80A/B/C/D1-107[»]
ProteinModelPortalQ7A649.
SMRQ7A649. Positions 1-107.
ModBaseSearch...

Protein-protein interaction databases

STRING158879.SA0983.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB42232; BAB42232; BAB42232.
GeneID1123810.
KEGGsau:SA0983.
PATRIC19574162. VBIStaAur116463_1051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
ProtClustDBPRK13312.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-1039-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. Dimer_A_B_barrel. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ7A649.

Entry information

Entry nameHDOX1_STAAN
AccessionPrimary (citable) accession number: Q7A649
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: May 1, 2013
This is version 62 of the entry and version 2 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

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