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Protein

Heme oxygenase (staphylobilin-producing) 1

Gene

isdG

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 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 stabilizerUniRule annotation
Metal bindingi77 – 771Iron (heme axial ligand)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1039-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:SA0983
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751 Componenti: Chromosome

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: Absence of oxygenase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Heme oxygenase (staphylobilin-producing) 1PRO_0000270091Add
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 – 227Combined sources
Helixi29 – 313Combined sources
Beta strandi35 – 439Combined sources
Beta strandi47 – 5913Combined sources
Helixi61 – 688Combined sources
Helixi71 – 777Combined sources
Turni83 – 853Combined sources
Beta strandi91 – 10616Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7A649.

Family & Domainsi

Domains and Repeats

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

Region

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

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.
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.

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

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42232.1. Different initiation.
PIRiD89884.
RefSeqiWP_000670950.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42232; BAB42232; BAB42232.
GeneIDi23196944.
PATRICi19574162. VBIStaAur116463_1051.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42232.1. Different initiation.
PIRiD89884.
RefSeqiWP_000670950.1. NC_002745.2.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB42232; BAB42232; BAB42232.
GeneIDi23196944.
PATRICi19574162. VBIStaAur116463_1051.

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
OrthoDBiEOG6GTZMS.

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1039-MONOMER.
BRENDAi1.14.99.48. 3352.

Miscellaneous databases

EvolutionaryTraceiQ7A649.

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: 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: July 22, 2015
This is version 77 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

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.