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Protein

Heme oxygenase (staphylobilin-producing) 1

Gene

isdG

Organism
Staphylococcus aureus (strain MW2)
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 annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71IronUniRule annotation
Sitei67 – 671Transition state stabilizerUniRule annotation
Metal bindingi77 – 771Iron (heme axial ligand)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciSAUR196620:GJ9Z-1042-MONOMER.
BRENDAi1.14.99.48. 3352.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase (staphylobilin-producing) 1UniRule annotation (EC:1.14.99.48UniRule annotation)
Alternative name(s):
Heme-degrading monooxygenase 1UniRule annotation
Iron-regulated surface determinant 1UniRule annotation
Iron-responsive surface determinant 1UniRule annotation
Gene namesi
Name:isdG
Ordered Locus Names:MW1018
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71N → A: Loss of activity. 1 Publication
Mutagenesisi17 – 171K → A: No effect. 1 Publication
Mutagenesisi23 – 231F → A: No effect. 1 Publication
Mutagenesisi38 – 381M → A: Slight loss of activity. Changes in heme binding. 1 Publication
Mutagenesisi67 – 671W → A: Loss of activity. 1 Publication
Mutagenesisi70 – 701S → A: No effect. 1 Publication
Mutagenesisi77 – 771H → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Heme oxygenase (staphylobilin-producing) 1PRO_0000270089Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210Combined sources
Helixi16 – 216Combined sources
Helixi29 – 313Combined sources
Beta strandi35 – 4511Combined sources
Beta strandi47 – 6014Combined sources
Helixi61 – 688Combined sources
Helixi71 – 799Combined sources
Turni83 – 853Combined sources
Beta strandi91 – 10616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XBWX-ray1.90A/B/C/D1-107[»]
ProteinModelPortaliQ8NX62.
SMRiQ8NX62. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NX62.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 9290ABMUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 298Heme bindingUniRule annotation

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.
OMAiGEGERIM.
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.

Q8NX62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD
60 70 80 90 100
EVKILTVWKS KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD

IGYSYMK
Length:107
Mass (Da):12,546
Last modified:October 1, 2002 - v1
Checksum:iDB13A134D5EC4FF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB94883.1.
RefSeqiNP_645835.1. NC_003923.1.
WP_000670950.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB94883; BAB94883; BAB94883.
GeneIDi23196944.
KEGGisam:MW1018.
PATRICi19568616. VBIStaAur44266_1067.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB94883.1.
RefSeqiNP_645835.1. NC_003923.1.
WP_000670950.1. NC_003923.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XBWX-ray1.90A/B/C/D1-107[»]
ProteinModelPortaliQ8NX62.
SMRiQ8NX62. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB94883; BAB94883; BAB94883.
GeneIDi23196944.
KEGGisam:MW1018.
PATRICi19568616. VBIStaAur44266_1067.

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
KOiK07145.
OMAiGEGERIM.
OrthoDBiEOG6GTZMS.

Enzyme and pathway databases

BioCyciSAUR196620:GJ9Z-1042-MONOMER.
BRENDAi1.14.99.48. 3352.

Miscellaneous databases

EvolutionaryTraceiQ8NX62.

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: MW2.
  2. "Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases."
    Wu R., Skaar E.P., Zhang R., Joachimiak G., Gornicki P., Schneewind O., Joachimiak A.
    J. Biol. Chem. 280:2840-2846(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-7; LYS-17; PHE-23; MET-38; TRP-67; SER-70 AND HIS-77.

Entry informationi

Entry nameiHDOX1_STAAW
AccessioniPrimary (citable) accession number: Q8NX62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2002
Last modified: June 24, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

IsdG seems to carry out oxygenation of the heme without the assistance of any of the prosthetic groups or cofactors normally associated with activation of molecular oxygen.

Keywords - Technical termi

3D-structure

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.