Heme-degrading monooxygenase 2 - Staphylococcus aureus (strain N315)

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Q7A827 (HDOX2_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Heme-degrading monooxygenase 2
EC=1.14.99.-

Alternative name(s):
Heme oxygenase 2
Iron-regulated surface determinant 2
Iron-responsive surface determinant 2

Gene names

Name:	isdI
Ordered Locus Names:	SA0160

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length	108 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Heme + 3 AH₂ + 3 O₂ = staphylobilins + Fe²⁺ + CO + 3 A + 3 H₂O. Ref.4
Subunit structure	Homodimer. Ref.3 Ref.4 Ref.5 Ref.6
Subcellular location	Cytoplasm By similarity.
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	3D-structure 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 – 108

108

Heme-degrading monooxygenase 2 HAMAP-Rule MF_01272

PRO_0000270092

Regions

Region

21 – 28

Heme binding HAMAP-Rule MF_01272

Sites

Metal binding

Iron

Metal binding

Iron (heme axial ligand)

Site

Transition state stabilizer

Experimental info

Mutagenesis

W → A: Inactive. Ref.6

Mutagenesis

W → F: Heme degradation activity is approximately half that of the wild-type enzyme. Ref.6

Mutagenesis

W → L: Inactive. Ref.6

Mutagenesis

W → 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

Length

Mass (Da)

Tools

Q7A827 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 8AF2718571451004
Show »

FASTA

108

12,791

        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' referencesShow '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. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000018 Genomic DNA. Translation: BAB41380.1.

PIR

A89778.

RefSeq

NP_373402.1. NC_002745.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZDP	X-ray	1.50	A/B	1-108	[»]
3LGM	X-ray	1.88	A/B	1-108	[»]
3LGN	X-ray	1.50	A/B	1-108	[»]
3QGP	X-ray	1.80	A/B	1-108	[»]
4FNH	X-ray	1.90	A/B	1-108	[»]
4FNI	X-ray	1.80	A/B	1-108	[»]

ProteinModelPortal

Q7A827.

SMR

Q7A827. Positions 1-108.

ModBase

Search...

Protein-protein interaction databases

STRING

158879.SA0160.

Proteomic databases

PRIDE

Q7A827.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAB41380; BAB41380; BAB41380.

GeneID

1122935.

KEGG

sau:SA0160.

PATRIC

19572351. VBIStaAur116463_0165.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG2329.

HOGENOM

HOG000008026.

K07145.

OMA

VTNTSKI.

ProtClustDB

PRK13313.

Enzyme and pathway databases

BioCyc

SAUR158879:GJCB-165-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...

Other

EvolutionaryTrace

Q7A827.

Entry information

Entry name

HDOX2_STAAN

Accession

Primary (citable) accession number: Q7A827

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents