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Q812Q3 (HDOX_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heme-degrading monooxygenase

EC=1.14.99.3
Alternative name(s):
Heme oxygenase
Iron-regulated surface determinant
Iron-responsive surface determinant
Gene names
Name:isdG
Ordered Locus Names:BC_4542
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length107 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the biliverdin in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron By similarity. HAMAP-Rule MF_01272

Catalytic activity

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. HAMAP-Rule MF_01272

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01272

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01272.

Sequence similarities

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheme catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron assimilation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheme binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

heme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 107107Heme-degrading monooxygenase HAMAP-Rule MF_01272
PRO_0000270072

Sites

Metal binding61Iron By similarity
Metal binding761Iron (heme axial ligand) By similarity
Site661Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q812Q3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E98EA5B28C19575C

FASTA10712,034
        10         20         30         40         50         60 
MIIVTNTAKI TKGNGHKLIE RFNKVGKVET MPGFLGLEVL LTQNTVDYDE VTISTRWNAK 

        70         80         90        100 
EDFQGWTKSA AFKDAHSHQG GMPEYILDNK IAYYDVKVVR MPMAAAQ 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP11450.1.
RefSeqNP_834249.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ812Q3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC4542.

Proteomic databases

PRIDEQ812Q3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP11450; AAP11450; BC_4542.
GeneID1206887.
KEGGbce:BC4542.
PATRIC32605203. VBIBacCer54481_4700.

Phylogenomic databases

eggNOGCOG2329.
KOK07145.
OMAISTRWKE.
OrthoDBEOG6GTZMS.
ProtClustDBPRK13314.

Enzyme and pathway databases

BioCycBCER226900:GJEU-4538-MONOMER.

Family and domain databases

HAMAPMF_01272. Heme_degrading_monooxygenase.
InterProIPR007138. Antibiotic_mOase.
IPR011008. Dimeric_a/b-barrel.
IPR023953. Heme-degrad_mOase.
[Graphical view]
PfamPF03992. ABM. 1 hit.
[Graphical view]
SUPFAMSSF54909. SSF54909. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHDOX_BACCR
AccessionPrimary (citable) accession number: Q812Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families