ID   HMOX_TAKRU              Reviewed;         277 AA.
AC   O73688;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Heme oxygenase;
DE            Short=HO;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN   Name=hmox;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9503016; DOI=10.1006/geno.1997.5162;
RA   Gottgens B., Gilbert J.G.R., Barton L.M., Aparicio S., Hawker K.,
RA   Mistry S., Vaudin M., King A., Bentley D., Elgar G., Green A.R.;
RT   "The pufferfish SLP-1 gene, a new member of the SCL/TAL-1 family of
RT   transcription factors.";
RL   Genomics 48:52-62(1998).
CC   -!- FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene
CC       bridge to form biliverdin. Biliverdin is subsequently converted to
CC       bilirubin by biliverdin reductase. Under physiological conditions, the
CC       activity of heme oxygenase is highest in the spleen, where senescent
CC       erythrocytes are sequestrated and destroyed. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC         biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:60344; EC=1.14.14.18;
CC         Evidence={ECO:0000250|UniProtKB:O48782};
CC   -!- SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR   EMBL; AF022814; AAC41263.1; -; Genomic_DNA.
DR   AlphaFoldDB; O73688; -.
DR   SMR; O73688; -.
DR   STRING; 31033.ENSTRUP00000011176; -.
DR   eggNOG; KOG4480; Eukaryota.
DR   InParanoid; O73688; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR   CDD; cd19165; HemeO; 1.
DR   Gene3D; 1.20.910.10; -; 1.
DR   InterPro; IPR002051; Haem_Oase.
DR   InterPro; IPR016053; Haem_Oase-like.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR018207; Haem_oxygenase_CS.
DR   PANTHER; PTHR10720; PTHR10720; 1.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   PIRSF; PIRSF000343; Haem_Oase; 1.
DR   PRINTS; PR00088; HAEMOXYGNASE.
DR   SUPFAM; SSF48613; SSF48613; 1.
DR   PROSITE; PS00593; HEME_OXYGENASE; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..277
FT                   /note="Heme oxygenase"
FT                   /id="PRO_0000209697"
FT   BINDING         29
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  31211 MW;  77B3584699963F77 CRC64;
     MEADKKTTAQ TESNRDLSEQ IKKVTKDVHV RAESTELMLS FQRGQVTLQQ YKLLLCSLYE
     IYLALEEEMD RNCDHPSVAP IYFPAELARL ATIEKDLEFF FGPDWREKIV VPAATERYCH
     RIRQIGQENP EYLIAHAYTR YLGDLSGGQV LGRIAQKSMK LGGSEGLSFF AFPGVSSPNL
     FKRLYRSRMN SVELTEEQRS AVLQEALGAF EFNIQVFEDL QKMLNVTENE PGVGTPRSRP
     ATTLQVGGSM IQTNPLFRMV LGLCLALATV SIGLYAL