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A0AFT8 (HDOX_LISW6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:lwe0452
OrganismListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334) [Complete proteome] [HAMAP]
Taxonomic identifier386043 [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

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
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 – 121121Heme-degrading monooxygenase HAMAP-Rule MF_01272
PRO_1000067383

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A0AFT8 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 956031E4F8DA2D49

FASTA12113,845
        10         20         30         40         50         60 
MIIVTNTIKV EKGAAEHVIR QFTGANGDGH PTKDIAEVEG FLGFELWHSK PEDKDYEEVV 

        70         80         90        100        110        120 
VTSKWESEEA QRNWVKSDSF KKAHGRTKDT REQREDRKGI VGNEIARFEV VHVQNPVTIE 


K 

« Hide

References

[1]"Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T. expand/collapse author list , Lampidis R., Kreft J., Goebel W., Chakraborty T.
J. Bacteriol. 188:7405-7415(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35897 / DSM 20650 / SLCC5334.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM263198 Genomic DNA. Translation: CAK19870.1.
RefSeqYP_848653.1. NC_008555.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386043.lwe0452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK19870; CAK19870; lwe0452.
GeneID4464193.
KEGGlwe:lwe0452.
PATRIC20328029. VBILisWel39304_0455.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
OMAISTRWKE.
OrthoDBEOG6GTZMS.
ProtClustDBPRK13316.

Enzyme and pathway databases

BioCycLWEL386043:GI5X-468-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_LISW6
AccessionPrimary (citable) accession number: A0AFT8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 28, 2006
Last modified: February 19, 2014
This is version 50 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