ID G5BPF0_HETGA Unreviewed; 374 AA.
AC G5BPF0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Heme oxygenase 1 {ECO:0000256|ARBA:ARBA00040247};
DE EC=1.14.14.18 {ECO:0000256|ARBA:ARBA00012360};
GN ORFNames=GW7_07170 {ECO:0000313|EMBL:EHB11161.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB11161.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB11161.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- FUNCTION: Catalyzes the oxidative cleavage of heme at the alpha-methene
CC bridge carbon, released as carbon monoxide (CO), to generate biliverdin
CC IXalpha, while releasing the central heme iron chelate as ferrous iron.
CC {ECO:0000256|ARBA:ARBA00037361}.
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|ARBA:ARBA00036473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC Evidence={ECO:0000256|ARBA:ARBA00036473};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00037869}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00037869}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00037869}.
CC -!- SIMILARITY: Belongs to the heme oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006134}.
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DR EMBL; JH171263; EHB11161.1; -; Genomic_DNA.
DR AlphaFoldDB; G5BPF0; -.
DR STRING; 10181.G5BPF0; -.
DR eggNOG; KOG4480; Eukaryota.
DR InParanoid; G5BPF0; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006788; P:heme oxidation; IEA:InterPro.
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:SF1; HEME OXYGENASE 1; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR PROSITE; PS00593; HEME_OXYGENASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 313..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 42182 MW; 068C9CB9B62F19D1 CRC64;
MKRVGDLFRA KPLALVPRWK VTCSTPLLHR DDWGPGIPGL VGAVFAELRV EPRARPRSLP
TLPRFGDPVV WSTWWALHPT NALTDPTLHR APQDLSEAIK ETTRDVHTQA ENTEFMRNFQ
KGQVTREGFK LVMASLYHVY VALEEEIERI RDSQVFAPVY FPEELHRRLA LEQDMAFWYG
PRWRHTIPCS PATSRYVQRI HEVGRMEPEL LVAHTYTRYL GDLSGGQVLK RIAQKALGLP
GSGEGLAFFT FPGIPNATKF KQLYRARMNS LEMTPEVRRR VLQEAKAAFH ACALVFQLFE
ELQGLLTPEL QDQSPPQTLG LHHRASSQVQ DSSPAEAPLS KAPLPSHVPA PLLPWVLTLL
SFLVATVAVG LYAL
//
