ID   HO_RHOVL                Reviewed;         235 AA.
AC   O19998;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   22-FEB-2023, entry version 79.
DE   RecName: Full=Heme oxygenase;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN   Name=pbsA;
OS   Rhodella violacea (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Rhodellophyceae; Rhodellales; Rhodellaceae;
OC   Rhodella.
OX   NCBI_TaxID=2801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9326680; DOI=10.1073/pnas.94.21.11736;
RA   Richaud C., Zabulon G.;
RT   "The heme oxygenase gene (pbsA) in the red alga Rhodella violacea is
RT   discontinuous and transcriptionally activated during iron limitation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11736-11741(1997).
CC   -!- FUNCTION: Catalyzes the opening of the heme ring with the release of
CC       iron. Key enzyme in the synthesis of the chromophoric part of the
CC       photosynthetic antennae.
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:0000250|UniProtKB:O48782};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR   EMBL; AF000719; AAB66516.1; -; Genomic_DNA.
DR   EMBL; AF000717; AAB66516.1; JOINED; Genomic_DNA.
DR   EMBL; AF000718; AAB66516.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; O19998; -.
DR   SMR; O19998; -.
DR   GO; GO:0009507; C:chloroplast; 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   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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: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.
DR   PROSITE; PS00593; HEME_OXYGENASE; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Heme; Iron; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Plastid.
FT   CHAIN           1..235
FT                   /note="Heme oxygenase"
FT                   /id="PRO_0000209700"
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:0000250"
SQ   SEQUENCE   235 AA;  27144 MW;  F0E797F8D5B72845 CRC64;
     MIYDTNLALQ LRQGTTKAHS MAENVSFVKS FLGGVVDKQA YRQLIANFYF VYSAIEDEMK
     RHQESQIIKP IYFEELNRKS SLEEDLQFYY GLEWQDKIFP SPATKVYINR IHEISNTSPE
     LLIAHCYTRY LGDLSGGQIL KKITQSAMNL SGGEGTAFYE FKDIKDEKNF KQNYRLALDS
     IHLSDSAIKS IVSEANIAFK LNMKIFQELN SNFIKIIAIF LFNFIKRIKL PGFKS
//