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Q6GHV0 (HDOX1_STAAR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:SAR1109
OrganismStaphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]
Taxonomic identifier282458 [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

Heme + 3 AH2 + 3 O2 = staphylobilins + Fe2+ + CO + 3 A + 3 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 107107Heme-degrading monooxygenase 1 HAMAP-Rule MF_01272
PRO_0000270083

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
Q6GHV0 [UniParc].

Last modified July 19, 2004. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571856 Genomic DNA. Translation: CAG40111.1.
RefSeqYP_040522.1. NC_002952.2.

3D structure databases

ProteinModelPortalQ6GHV0.
SMRQ6GHV0. Positions 1-107.
ModBaseSearch...

Protein-protein interaction databases

STRING282458.SAR1109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG40111; CAG40111; SAR1109.
GeneID2860363.
KEGGsar:SAR1109.
PATRIC19545761. VBIStaAur71814_1111.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK00510.
OMAGEGERIM.
ProtClustDBPRK13312.

Enzyme and pathway databases

BioCycSAUR282458:GJA5-1109-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...

Entry information

Entry nameHDOX1_STAAR
AccessionPrimary (citable) accession number: Q6GHV0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 19, 2004
Last modified: May 1, 2013
This is version 63 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