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Q8NX62

- HDOX1_STAAW

UniProt

Q8NX62 - HDOX1_STAAW

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Protein
Heme oxygenase (staphylobilin-producing) 1
Gene
isdG, MW1018
Organism
Staphylococcus aureus (strain MW2)
Status
Reviewed - 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 By similarity.1 Publication

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 – 71Iron By similarity
Sitei67 – 671Transition state stabilizer By similarity
Metal bindingi77 – 771Iron (heme axial ligand) By similarity

GO - Molecular functioni

  1. heme binding Source: UniProtKB-HAMAP
  2. heme oxygenase (decyclizing) activity Source: UniProtKB-HAMAP
  3. iron ion binding Source: UniProtKB-HAMAP
  4. monooxygenase activity Source: UniProtKB-KW

GO - Biological processi

  1. heme catabolic process Source: UniProtKB-HAMAP
  2. iron assimilation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciSAUR196620:GJ9Z-1042-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase (staphylobilin-producing) 1 (EC:1.14.99.48)
Alternative name(s):
Heme oxygenase 1
Heme-degrading monooxygenase 1
Iron-regulated surface determinant 1
Iron-responsive surface determinant 1
Gene namesi
Name:isdG
Ordered Locus Names:MW1018
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000418: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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) 1UniRule annotation
PRO_0000270089Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi196620.MW1018.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XBWX-ray1.90A/B/C/D1-107[»]
ProteinModelPortaliQ8NX62.
SMRiQ8NX62. Positions 1-107.

Miscellaneous databases

EvolutionaryTraceiQ8NX62.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 298Heme binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
KOiK07145.
OMAiVRHQSQD.
OrthoDBiEOG6GTZMS.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q8NX62-1 [UniParc]FASTAAdd to Basket

« Hide

MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD    50
EVKILTVWKS KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD 100
IGYSYMK 107
Length:107
Mass (Da):12,546
Last modified:October 1, 2002 - v1
Checksum:iDB13A134D5EC4FF0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000033 Genomic DNA. Translation: BAB94883.1.
RefSeqiNP_645835.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB94883; BAB94883; BAB94883.
GeneIDi1003130.
KEGGisam:MW1018.
PATRICi19568616. VBIStaAur44266_1067.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000033 Genomic DNA. Translation: BAB94883.1 .
RefSeqi NP_645835.1. NC_003923.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XBW X-ray 1.90 A/B/C/D 1-107 [» ]
ProteinModelPortali Q8NX62.
SMRi Q8NX62. Positions 1-107.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196620.MW1018.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB94883 ; BAB94883 ; BAB94883 .
GeneIDi 1003130.
KEGGi sam:MW1018.
PATRICi 19568616. VBIStaAur44266_1067.

Phylogenomic databases

eggNOGi COG2329.
HOGENOMi HOG000008026.
KOi K07145.
OMAi VRHQSQD.
OrthoDBi EOG6GTZMS.

Enzyme and pathway databases

BioCyci SAUR196620:GJ9Z-1042-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q8NX62.

Family and domain databases

HAMAPi MF_01272. Heme_degrading_monooxygenase.
InterProi IPR007138. ABM-like.
IPR011008. Dimeric_a/b-barrel.
IPR023953. IsdG.
[Graphical view ]
Pfami PF03992. ABM. 1 hit.
[Graphical view ]
SUPFAMi SSF54909. SSF54909. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 76 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, 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

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