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Q92EH3 (HDOX_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. 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:lmo0484
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length121 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 – 121121Heme-degrading monooxygenase HAMAP-Rule MF_01272
PRO_0000270078

Sites

Metal binding61Iron By similarity
Metal binding841Iron (heme axial ligand) By similarity
Site741Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92EH3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 95674EA508DA2D49

FASTA12113,785
        10         20         30         40         50         60 
MIIVTNTIKV EKGAAEHVIR QFTGANGDGH PTKDIAEVEG FLGFELWHSK PEDKDYEEVV 

        70         80         90        100        110        120 
VTSKWESEEA QRNWVKSDSF KKAHGRTKDT REQREDRKGI VGNAIARFEV VHVQNPVIVE 


K 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591975 Genomic DNA. Translation: CAC98563.1.
PIRAE1135.
AG1493.
RefSeqNP_464012.1. NC_003210.1.

3D structure databases

ProteinModelPortalQ92EH3.
ModBaseSearch...

Protein-protein interaction databases

STRING169963.lmo0484.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC98563; CAC98563; CAC98563.
GeneID985220.
KEGGlmo:lmo0484.
PATRIC20310035. VBILisMon69206_0503.

Organism-specific databases

GenoListLMO0484.

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
OMAVTNTSKI.
ProtClustDBPRK13316.

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_LISMO
AccessionPrimary (citable) accession number: Q92EH3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 67 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