ID A0A091FQG2_9AVES Unreviewed; 312 AA.
AC A0A091FQG2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Heme oxygenase {ECO:0000256|PIRNR:PIRNR000343};
DE EC=1.14.14.18 {ECO:0000256|PIRNR:PIRNR000343};
GN ORFNames=N303_04361 {ECO:0000313|EMBL:KFO71206.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO71206.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO71206.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO71206.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00006134, ECO:0000256|PIRNR:PIRNR000343}.
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DR EMBL; KL447254; KFO71206.1; -; Genomic_DNA.
DR RefSeq; XP_009569269.1; XM_009570974.1.
DR AlphaFoldDB; A0A091FQG2; -.
DR STRING; 55661.A0A091FQG2; -.
DR KEGG; cuca:104068127; -.
DR OrthoDB; 1366343at2759; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
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 InterPro; IPR018207; Haem_oxygenase_CS.
DR PANTHER; PTHR10720; HEME OXYGENASE; 1.
DR PANTHER; PTHR10720:SF2; HEME OXYGENASE 2; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PIRSF; PIRSF000343; Haem_Oase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR PROSITE; PS00593; HEME_OXYGENASE; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000343};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000343};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000343};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 44
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 153
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 202
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 312 AA; 35506 MW; 8C490F7F5ACE859A CRC64;
MPSAMEGSEA GEEGEILRYE ETDDDNVSPT DLSELLKEGT KESHDRAENT QFVKDFLKGR
IRKELFKLAT VALYFTYSAL EEEIDRNKDN PVFAPLYFPL ELHRREALVK DLQYFYGEDW
KEKIQCSEAT QHYVDRIHHV GQHEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTE
EGIQFYVFDN ISNAQQFKQL YRARMNALDL DKNTKDRIVE EANRAFRFNM QVFDELDQLG
KSLTEEAQDG DLPVHDGKGD VRKCPYYADK LGQMGPSCPY HAAVALVKQP LVQLILAACI
AVAAGAAAWY VM
//
