Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2FZE2

- HDOX1_STAA8

UniProt

Q2FZE2 - HDOX1_STAA8

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Heme oxygenase (staphylobilin-producing) 1

Gene

isdG

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed - Annotation score: 4 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.1 PublicationUniRule annotation
Protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O.1 PublicationUniRule 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

  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

BioCyciSAUR93061:GIWJ-1047-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase (staphylobilin-producing) 1UniRule annotation (EC:1.14.99.48)
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:SAOUHSC_01089
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000008816: Chromosome

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Heme oxygenase (staphylobilin-producing) 1PRO_0000270093Add
BLAST

Expressioni

Inductioni

Transcriptionally regulated by iron and the ferric uptake repressor (fur) protein.1 Publication

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi93061.SAOUHSC_01089.

Structurei

3D structure databases

ProteinModelPortaliQ2FZE2.
SMRiQ2FZE2. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

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.
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.
PROSITEiPS51725. ABM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2FZE2-1 [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:March 21, 2006 - v1
Checksum:iDB13A134D5EC4FF0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000253 Genomic DNA. Translation: ABD30204.1.
RefSeqiYP_499634.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD30204; ABD30204; SAOUHSC_01089.
GeneIDi3919250.
KEGGisao:SAOUHSC_01089.
PATRICi19579679. VBIStaAur99865_0998.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000253 Genomic DNA. Translation: ABD30204.1 .
RefSeqi YP_499634.1. NC_007795.1.

3D structure databases

ProteinModelPortali Q2FZE2.
SMRi Q2FZE2. Positions 1-107.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 93061.SAOUHSC_01089.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD30204 ; ABD30204 ; SAOUHSC_01089 .
GeneIDi 3919250.
KEGGi sao:SAOUHSC_01089.
PATRICi 19579679. VBIStaAur99865_0998.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SAUR93061:GIWJ-1047-MONOMER.

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.
PROSITEi PS51725. ABM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Staphylococcus aureus NCTC 8325 genome."
    Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
    (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 8325.
  2. "IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus."
    Skaar E.P., Gaspar A.H., Schneewind O.
    J. Biol. Chem. 279:436-443(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiHDOX1_STAA8
AccessioniPrimary (citable) accession number: Q2FZE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: March 21, 2006
Last modified: October 29, 2014
This is version 62 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3