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Protein

Heme oxygenase (staphylobilin-producing) 2

Gene

isdI

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation2 Publications

Catalytic activityi

Protoheme + 4 AH2 + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.UniRule annotation1 Publication
Protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi6 – 61Iron
Sitei66 – 661Transition state stabilizer
Metal bindingi76 – 761Iron (heme axial ligand)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-165-MONOMER.
BRENDAi1.14.99.48. 3352.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase (staphylobilin-producing) 2UniRule annotation (EC:1.14.99.48)
Alternative name(s):
Heme-degrading monooxygenase 2UniRule annotation
Iron-regulated surface determinant 2UniRule annotation
Iron-responsive surface determinant 2UniRule annotation
Gene namesi
Name:isdI
Ordered Locus Names:SA0160
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661W → A: Inactive. 1 Publication
Mutagenesisi66 – 661W → F: Heme degradation activity is approximately half that of the wild-type enzyme. 1 Publication
Mutagenesisi66 – 661W → L: Inactive. 1 Publication
Mutagenesisi66 – 661W → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108108Heme oxygenase (staphylobilin-producing) 2PRO_0000270092Add
BLAST

Proteomic databases

PRIDEiQ7A827.

Interactioni

Subunit structurei

Homodimer.UniRule annotation4 Publications

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi15 – 206Combined sources
Helixi21 – 233Combined sources
Helixi28 – 303Combined sources
Beta strandi34 – 429Combined sources
Beta strandi47 – 5812Combined sources
Helixi60 – 678Combined sources
Helixi70 – 756Combined sources
Turni76 – 783Combined sources
Beta strandi92 – 10716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZDPX-ray1.50A/B1-108[»]
3LGMX-ray1.88A/B1-108[»]
3LGNX-ray1.50A/B1-108[»]
3QGPX-ray1.80A/B1-108[»]
4FNHX-ray1.90A/B1-108[»]
4FNIX-ray1.80A/B1-108[»]
ProteinModelPortaliQ7A827.
SMRiQ7A827. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7A827.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 9392ABMUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 288Heme binding

Sequence similaritiesi

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.UniRule annotation
Contains 1 ABM domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
KOiK07145.
OMAiISTRWKE.
OrthoDBiEOG6GTZMS.

Family and domain databases

HAMAPiMF_01272. Heme_degrading_monooxygenase.
InterProiIPR007138. ABM_dom.
IPR011008. Dimeric_a/b-barrel.
IPR023953. IsdG.
[Graphical view]
PfamiPF03992. ABM. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
PROSITEiPS51725. ABM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7A827-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE
60 70 80 90 100
VKILTIWESE DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY

DIGYHYQK
Length:108
Mass (Da):12,791
Last modified:July 5, 2004 - v1
Checksum:i8AF2718571451004
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB41380.1.
PIRiA89778.
RefSeqiWP_000480603.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB41380; BAB41380; BAB41380.
GeneIDi23195987.
KEGGisau:SA0160.
PATRICi19572351. VBIStaAur116463_0165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB41380.1.
PIRiA89778.
RefSeqiWP_000480603.1. NC_002745.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZDPX-ray1.50A/B1-108[»]
3LGMX-ray1.88A/B1-108[»]
3LGNX-ray1.50A/B1-108[»]
3QGPX-ray1.80A/B1-108[»]
4FNHX-ray1.90A/B1-108[»]
4FNIX-ray1.80A/B1-108[»]
ProteinModelPortaliQ7A827.
SMRiQ7A827. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ7A827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB41380; BAB41380; BAB41380.
GeneIDi23195987.
KEGGisau:SA0160.
PATRICi19572351. VBIStaAur116463_0165.

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
KOiK07145.
OMAiISTRWKE.
OrthoDBiEOG6GTZMS.

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-165-MONOMER.
BRENDAi1.14.99.48. 3352.

Miscellaneous databases

EvolutionaryTraceiQ7A827.

Family and domain databases

HAMAPiMF_01272. Heme_degrading_monooxygenase.
InterProiIPR007138. ABM_dom.
IPR011008. Dimeric_a/b-barrel.
IPR023953. IsdG.
[Graphical view]
PfamiPF03992. ABM. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
PROSITEiPS51725. ABM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.

Entry informationi

Entry nameiHDOX2_STAAN
AccessioniPrimary (citable) accession number: Q7A827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.