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Q7A649

- HDOX1_STAAN

UniProt

Q7A649 - HDOX1_STAAN

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Protein
Heme oxygenase (staphylobilin-producing) 1
Gene
isdG, SA0983
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 staphylobilins (a mixture of 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.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
Sitei67 – 671Transition state stabilizer Reviewed prediction
Metal bindingi77 – 771Iron (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-1039-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:SA0983
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
Mutagenesisi7 – 71N → A: Absence of oxygenase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Heme oxygenase (staphylobilin-producing) 1UniRule annotation
PRO_0000270091Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi158879.SA0983.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210
Helixi16 – 227
Helixi29 – 313
Beta strandi35 – 439
Beta strandi47 – 5913
Helixi61 – 688
Helixi71 – 777
Turni83 – 853
Beta strandi91 – 10616

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZDOX-ray1.80A/B/C/D1-107[»]
ProteinModelPortaliQ7A649.
SMRiQ7A649. Positions 1-107.

Miscellaneous databases

EvolutionaryTraceiQ7A649.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
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.

Q7A649-1 [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:January 9, 2007 - v2
Checksum:iDB13A134D5EC4FF0
GO

Sequence cautioni

The sequence BAB42232.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB42232.1. Different initiation.
PIRiD89884.

Genome annotation databases

EnsemblBacteriaiBAB42232; BAB42232; BAB42232.
PATRICi19574162. VBIStaAur116463_1051.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB42232.1 . Different initiation.
PIRi D89884.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZDO X-ray 1.80 A/B/C/D 1-107 [» ]
ProteinModelPortali Q7A649.
SMRi Q7A649. Positions 1-107.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158879.SA0983.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB42232 ; BAB42232 ; BAB42232 .
PATRICi 19574162. VBIStaAur116463_1051.

Phylogenomic databases

eggNOGi COG2329.
HOGENOMi HOG000008026.
OrthoDBi EOG6GTZMS.

Enzyme and pathway databases

BioCyci SAUR158879:GJCB-1039-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q7A649.

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. "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 (1.8 ANGSTROMS) OF MUTANT ALA-7 IN COMPLEX WITH HEME, FUNCTION, MUTAGENESIS OF ASN-7, SUBUNIT.

Entry informationi

Entry nameiHDOX1_STAAN
AccessioniPrimary (citable) accession number: Q7A649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: September 3, 2014
This is version 69 of the entry and version 2 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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