Q6GHV0 (HDOX1_STAAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	107 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	heme catabolic process Inferred from electronic annotation. Source: HAMAP iron assimilation Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	heme binding Inferred from electronic annotation. Source: HAMAP heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 107	107	Heme-degrading monooxygenase 1 HAMAP-Rule MF_01272		PRO_0000270083
Regions
	Region	22 – 29	8	Heme binding By similarity
Sites
	Metal binding	7	1	Iron By similarity
	Metal binding	77	1	Iron (heme axial ligand) By similarity
	Site	67	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GHV0 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: DB13A134D5EC4FF0	FASTA	107	12,546
	10 20 30 40 50 60 MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS 70 80 90 100 KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MRSA252.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571856 Genomic DNA. Translation: CAG40111.1.
RefSeq	YP_040522.1. NC_002952.2.
3D structure databases
ProteinModelPortal	Q6GHV0.
SMR	Q6GHV0. Positions 1-107.
ModBase	Search...
Protein-protein interaction databases
STRING	282458.SAR1109.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAG40111; CAG40111; SAR1109.
GeneID	2860363.
KEGG	sar:SAR1109.
PATRIC	19545761. VBIStaAur71814_1111.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2329.
HOGENOM	HOG000008026.
KO	K00510.
OMA	GEGERIM.
ProtClustDB	PRK13312.
Enzyme and pathway databases
BioCyc	SAUR282458:GJA5-1109-MONOMER.
Family and domain databases
HAMAP	MF_01272. Heme_degrading_monooxygenase.
InterPro	IPR007138. Antibiotic_mOase. IPR011008. Dimeric_a/b-barrel. IPR023953. Heme-degrad_mOase. [Graphical view]
Pfam	PF03992. ABM. 1 hit. [Graphical view]
SUPFAM	SSF54909. Dimer_A_B_barrel. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HDOX1_STAAR

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program