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Database: UniProt
Entry: A0A0Q3MQQ8_AMAAE
LinkDB: A0A0Q3MQQ8_AMAAE
Original site: A0A0Q3MQQ8_AMAAE 
ID   A0A0Q3MQQ8_AMAAE        Unreviewed;       301 AA.
AC   A0A0Q3MQQ8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Heme oxygenase {ECO:0000256|PIRNR:PIRNR000343};
DE            EC=1.14.14.18 {ECO:0000256|PIRNR:PIRNR000343};
GN   ORFNames=AAES_193161 {ECO:0000313|EMBL:KQK84832.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK84832.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK84832.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK84832.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK84832.1}.
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DR   EMBL; LMAW01000969; KQK84832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q3MQQ8; -.
DR   STRING; 12930.A0A0Q3MQQ8; -.
DR   Proteomes; UP000051836; 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:UP000051836};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         27
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT   BINDING         34
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         143
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT   BINDING         192
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ   SEQUENCE   301 AA;  34307 MW;  F21D4491801882DD CRC64;
     MLLHEPFSFY GVTMKGNHPT DLSELLKEGT KESHDRAENT QFVKDFLKGR IKEELFKLAT
     VALYFTYSAL EEEMDRNKDN PTFAPLYFPL ELHRKEALIK DLQYFYGEDW KEKIECSEAT
     QQYVDRIHHV GQNEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTE EGIQFYVFGN
     ISNAQQFKQL YRARMNTLDL DKNTKERIVE EANRAFRFNM QVFDELDKIG KSLAEAQDGG
     LPVHDGKGDL RKCPYYADKL GNAGHSCPYQ GTVALAKQPL VQLMLAACVA VLAGAAAWYM
     M
//
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