ID E2AD16_CAMFO Unreviewed; 253 AA.
AC E2AD16;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Heme oxygenase {ECO:0000256|PIRNR:PIRNR000343};
DE EC=1.14.14.18 {ECO:0000256|PIRNR:PIRNR000343};
GN ORFNames=EAG_14951 {ECO:0000313|EMBL:EFN68652.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN68652.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL438658; EFN68652.1; -; Genomic_DNA.
DR RefSeq; XP_011255812.1; XM_011257510.2.
DR AlphaFoldDB; E2AD16; -.
DR STRING; 104421.E2AD16; -.
DR EnsemblMetazoa; XM_011257510.3; XP_011255812.1; LOC105251022.
DR GeneID; 105251022; -.
DR KEGG; cfo:105251022; -.
DR InParanoid; E2AD16; -.
DR OMA; FAFAFQM; -.
DR OrthoDB; 1366343at2759; -.
DR Proteomes; UP000000311; 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:UP000000311};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 21
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 127
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 180
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 253 AA; 29270 MW; 595BEEED6F9322A2 CRC64;
MPSKGEENFC KKMARSTRGV HAISDALVNA KLAFGFLDDS VWADGLLVFY EVFRYLEGAM
IRLRNTKIGL LPLSELQRTE AFERDLDHYL GKEWRKNYSP RDSVTKYLMR LREIEDTDPT
LLMAYIYHLY MGLLSGGIIL RKKRQLMQKI SPFKASPSND GNSITDFGQN SIFQLKSDLR
ESMNRIAETL DEDTKNKLIE ESKIVFELNN EIVKSVQTGN HVFEKVLYFI GQIVLILCIL
IIVLNILFKY IIR
//
