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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)DescriptionActionsGraphical viewLength
Metal bindingi6Iron1
Sitei66Transition state stabilizer1
Metal bindingi76Iron (heme axial ligand)1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi66W → A: Inactive. 1 Publication1
Mutagenesisi66W → F: Heme degradation activity is approximately half that of the wild-type enzyme. 1 Publication1
Mutagenesisi66W → L: Inactive. 1 Publication1
Mutagenesisi66W → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002700921 – 108Heme oxygenase (staphylobilin-producing) 2Add BLAST108

Interactioni

Subunit structurei

Homodimer.UniRule annotation4 Publications

Structurei

Secondary structure

1108
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Helixi15 – 20Combined sources6
Helixi21 – 23Combined sources3
Helixi28 – 30Combined sources3
Beta strandi34 – 42Combined sources9
Beta strandi47 – 58Combined sources12
Helixi60 – 67Combined sources8
Helixi70 – 75Combined sources6
Turni76 – 78Combined sources3
Beta strandi92 – 107Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7A827.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 93ABMUniRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 28Heme binding8

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000008026.
KOiK07145.
OMAiISTRWKE.

Family and domain databases

HAMAPiMF_01272. Heme_degrading_monooxygenase. 1 hit.
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.
GeneIDi28379517.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB41380; BAB41380; BAB41380.
GeneIDi28379517.
KEGGisau:SA0160.
PATRICi19572351. VBIStaAur116463_0165.

Phylogenomic databases

HOGENOMiHOG000008026.
KOiK07145.
OMAiISTRWKE.

Enzyme and pathway databases

BRENDAi1.14.99.48. 3352.

Miscellaneous databases

EvolutionaryTraceiQ7A827.

Family and domain databases

HAMAPiMF_01272. Heme_degrading_monooxygenase. 1 hit.
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...

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: November 2, 2016
This is version 87 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

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 one 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.