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Q7A827

- HDOX2_STAAN

UniProt

Q7A827 - HDOX2_STAAN

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Protein
Heme oxygenase (staphylobilin-producing) 2
Gene
isdI, SA0160
Organism
Staphylococcus aureus (strain N315)
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.2 Publications

Catalytic activityi

Protoheme + 4 AH2 + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.1 Publication
Protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.1 Publication

Sites

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

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

BioCyciSAUR158879:GJCB-165-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase (staphylobilin-producing) 2 (EC:1.14.99.48)
Alternative name(s):
Heme oxygenase 2
Heme-degrading monooxygenase 2
Iron-regulated surface determinant 2
Iron-responsive surface determinant 2
Gene namesi
Name:isdI
Ordered Locus Names:SA0160
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751: 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
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) 2UniRule annotation
PRO_0000270092Add
BLAST

Proteomic databases

PRIDEiQ7A827.

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

STRINGi158879.SA0160.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ7A827.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
KOiK07145.
OMAiGICKTTH.
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.

Q7A827-1 [UniParc]FASTAAdd to Basket

« Hide

MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE    50
VKILTIWESE DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY 100
DIGYHYQK 108
Length:108
Mass (Da):12,791
Last modified:July 5, 2004 - v1
Checksum:i8AF2718571451004
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB41380.1.
PIRiA89778.
RefSeqiNP_373402.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB41380; BAB41380; BAB41380.
GeneIDi1122935.
KEGGisau:SA0160.
PATRICi19572351. VBIStaAur116463_0165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB41380.1 .
PIRi A89778.
RefSeqi NP_373402.1. NC_002745.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q7A827.
SMRi Q7A827. Positions 1-108.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158879.SA0160.

Proteomic databases

PRIDEi Q7A827.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB41380 ; BAB41380 ; BAB41380 .
GeneIDi 1122935.
KEGGi sau:SA0160.
PATRICi 19572351. VBIStaAur116463_0165.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SAUR158879:GJCB-165-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q7A827.

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: 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: September 3, 2014
This is version 73 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

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