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Q72ZK2 (HDOX_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:BCE_4666
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [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

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 107107Heme-degrading monooxygenase HAMAP-Rule MF_01272
PRO_0000270071

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q72ZK2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: ACB308A337A92DFB

FASTA10712,004
        10         20         30         40         50         60 
MIIVTNTAKI TKGNGHKLID RFNKVGQVET MPGFLGLEVL LTQNTVDYDE VTISTRWNAK 

        70         80         90        100 
EDFQGWTKSP AFKAAHSHQG GMPDYILDNK ISYYDVKVVR MPMAAAQ 

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References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS43567.1.
RefSeqNP_980959.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ72ZK2.
ModBaseSearch...

Protein-protein interaction databases

STRING222523.BCE_4666.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS43567; AAS43567; BCE_4666.
GeneID2749219.
KEGGbca:BCE_4666.
PATRIC18857946. VBIBacCer118379_4468.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
OMAVTNTSKI.
ProtClustDBPRK13314.

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. Dimer_A_B_barrel. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHDOX_BACC1
AccessionPrimary (citable) accession number: Q72ZK2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 60 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