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Q81L50 (HDOX_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:BA_4782, GBAA_4782, BAS4437
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length107 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.4

Catalytic activity

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. Ref.4

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01272

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01272.

Induction

Up-regulated under iron-starved conditions Probable. Ref.4

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_0000270070

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q81L50 [UniParc].

Last modified June 1, 2003. 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 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[3]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[4]"Bacillus anthracis IsdG, a heme-degrading monooxygenase."
Skaar E.P., Gaspar A.H., Schneewind O.
J. Bacteriol. 188:1071-1080(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP28473.1.
AE017225 Genomic DNA. Translation: AAT56735.1.
AE017334 Genomic DNA. Translation: AAT33903.1.
RefSeqNP_846987.1. NC_003997.3.
YP_021428.1. NC_007530.2.
YP_030684.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81L50.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198094.BA_4782.

Protocols and materials databases

DNASU1083895.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP28473; AAP28473; BA_4782.
AAT33903; AAT33903; GBAA_4782.
AAT56735; AAT56735; BAS4437.
GeneID1083895.
2815699.
2851618.
KEGGban:BA_4782.
bar:GBAA_4782.
bat:BAS4437.

Phylogenomic databases

eggNOGCOG2329.
HOGENOMHOG000008026.
KOK07145.
OMASARISFR.
OrthoDBEOG6GTZMS.

Enzyme and pathway databases

BioCycBANT260799:GJAJ-4494-MONOMER.
BANT261594:GJ7F-4645-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_BACAN
AccessionPrimary (citable) accession number: Q81L50
Secondary accession number(s): Q6HSK4, Q6KLU7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 82 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