ID A0A195EDG8_9HYME Unreviewed; 251 AA.
AC A0A195EDG8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Heme oxygenase {ECO:0000256|PIRNR:PIRNR000343};
DE EC=1.14.14.18 {ECO:0000256|PIRNR:PIRNR000343};
GN ORFNames=ALC57_04126 {ECO:0000313|EMBL:KYN23253.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN23253.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN23253.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN23253.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN23253.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-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|PIRNR:PIRNR000343}.
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DR EMBL; KQ979039; KYN23253.1; -; Genomic_DNA.
DR RefSeq; XP_018358787.1; XM_018503285.1.
DR AlphaFoldDB; A0A195EDG8; -.
DR STRING; 471704.A0A195EDG8; -.
DR GeneID; 108758374; -.
DR OrthoDB; 1366343at2759; -.
DR Proteomes; UP000078492; 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 PANTHER; PTHR10720; HEME OXYGENASE; 1.
DR PANTHER; PTHR10720:SF0; HEME OXYGENASE; 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 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:UP000078492};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 224..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 19
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 125
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 178
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 251 AA; 29141 MW; E6D45F5B748E90C5 CRC64;
MPEEENFCKK MSKATRGIHA ISDTLVNAKL AFGFLDDSVW ADGLLVFYEV FRYLEGAMIR
LRNTKIGLLP LSELQRTEAF ERDLDHYLGK GWRKNYSPRD SVAKYLMRLR EVEDTDPTLL
MAYIYHLYMG LLSGGIILRK KRQIVQKISP FKAQPSSDGN NVTDFGQNSI FQLKRELRES
MNRIAETLDE DTKNKLIEES KIVFELNNEI IKSVQTGSHV FEKIFYFIGP VLLVLFVLII
VLNILYKYII R
//
