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Database: UniProt
Entry: A0A3P8UC06_AMPPE
LinkDB: A0A3P8UC06_AMPPE
Original site: A0A3P8UC06_AMPPE 
ID   A0A3P8UC06_AMPPE        Unreviewed;       280 AA.
AC   A0A3P8UC06;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Heme oxygenase {ECO:0000256|PIRNR:PIRNR000343};
DE            EC=1.14.14.18 {ECO:0000256|PIRNR:PIRNR000343};
GN   Name=HMOX1 {ECO:0000313|Ensembl:ENSAPEP00000032827.1};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000032827.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000032827.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000032827.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000343};
CC   -!- SIMILARITY: Belongs to the heme oxygenase family.
CC       {ECO:0000256|PIRNR:PIRNR000343}.
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DR   AlphaFoldDB; A0A3P8UC06; -.
DR   STRING; 161767.ENSAPEP00000032827; -.
DR   Ensembl; ENSAPET00000033692.1; ENSAPEP00000032827.1; ENSAPEG00000023325.1.
DR   GeneTree; ENSGT00390000017673; -.
DR   OMA; FAYLHVM; -.
DR   Proteomes; UP000265080; Chromosome 3.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006788; P:heme oxidation; IEA:UniProtKB-UniRule.
DR   CDD; cd19165; HemeO; 1.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR   InterPro; IPR002051; Haem_Oase.
DR   InterPro; IPR016053; Haem_Oase-like.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   PANTHER; PTHR10720; HEME OXYGENASE; 1.
DR   PANTHER; PTHR10720:SF1; HEME OXYGENASE 1; 1.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   PIRSF; PIRSF000343; Haem_Oase; 1.
DR   PRINTS; PR00088; HAEMOXYGNASE.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Heme {ECO:0000256|PIRNR:PIRNR000343, ECO:0000256|PIRSR:PIRSR000343-1};
KW   Iron {ECO:0000256|PIRNR:PIRNR000343, ECO:0000256|PIRSR:PIRSR000343-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000343,
KW   ECO:0000256|PIRSR:PIRSR000343-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         23
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT   BINDING         30
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:0000256|PIRSR:PIRSR000343-2"
FT   BINDING         139
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT   BINDING         187
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ   SEQUENCE   280 AA;  31782 MW;  C57E0BCC3522916A CRC64;
     METEKTQTAA EQMTDRDLSE QIKKVTKESH VRAENTELML SFQRGKVTLP QYKLLLCSLY
     EIYQALEEEL DRNSNHPGVA PIYFPAELAR QESIEKDLEY FYGPDWREKI VVPAATKRYC
     HRLRQIGKEN PEFLLAHAYT RYLGDLSGGQ VLGRIAQKSM GLKNSEGLSF FAFPGVSSPN
     LFKQLYRSRM NSVELMEEER NGVLEEAVRA FEFNIQVFDD LQKLLSVTEN NLQSCLTHSK
     PVNAKGFQIP GTLISSSPLL RMVLGFFVAL ATVSVGIYAL
//
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