Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O73688 (HMOX_FUGRU)

Last modified June 16, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Heme oxygenase
      Short name=HO
    EC=1.14.99.3
Gene names
Name: hmox
OrganismFugu rubripes (Japanese pufferfish) (Takifugu rubripes)
Taxonomic identifier31033 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaAcanthopterygiiPercomorphaTetraodontiformesTetradontoideaTetraodontidaeTakifugu

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed By similarity.

Catalytic activity

Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Subcellular location

Microsome By similarity. Endoplasmic reticulum By similarity.

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processheme oxidation

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

microsome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Heme oxygenase
PRO_0000209697

Sites

Metal binding291Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
O73688-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 77B3584699963F77

FASTA27731,211
        10         20         30         40         50         60 
MEADKKTTAQ TESNRDLSEQ IKKVTKDVHV RAESTELMLS FQRGQVTLQQ YKLLLCSLYE 

        70         80         90        100        110        120 
IYLALEEEMD RNCDHPSVAP IYFPAELARL ATIEKDLEFF FGPDWREKIV VPAATERYCH 

       130        140        150        160        170        180 
RIRQIGQENP EYLIAHAYTR YLGDLSGGQV LGRIAQKSMK LGGSEGLSFF AFPGVSSPNL 

       190        200        210        220        230        240 
FKRLYRSRMN SVELTEEQRS AVLQEALGAF EFNIQVFEDL QKMLNVTENE PGVGTPRSRP 

       250        260        270 
ATTLQVGGSM IQTNPLFRMV LGLCLALATV SIGLYAL 

« Hide

References

[1]"The pufferfish SLP-1 gene, a new member of the SCL/TAL-1 family of transcription factors."
Gottgens B., Gilbert J.G.R., Barton L.M., Aparicio S., Hawker K., Mistry S., Vaudin M., King A., Bentley D., Elgar G., Green A.R.
Genomics 48:52-62(1998) [PubMed: 9503016] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AF022814 Genomic DNA. Translation: AAC41263.1.

3D structure databases

HSSPHSSP built from PDB template 1N45 based on UniProtKB P09601.
ModBaseSearch...

Phylogenomic databases

HOVERGENO73688.

Enzyme and pathway databases

BRENDA1.14.99.3. 281122.

Family and domain databases

InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
Gene3DG3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit.
PANTHERPTHR10720. Haem_Oase. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHMOX_FUGRU
AccessionPrimary (citable) accession number: O73688
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents