ID   HMOX1_ORYSJ             Reviewed;         289 AA.
AC   Q69XJ4; A0A0P0WYR3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Heme oxygenase 1, chloroplastic;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
DE   AltName: Full=Protein PHOTOPERIODIC SENSITIVITY 5;
DE   Flags: Precursor;
GN   Name=HO1; Synonyms=HY1, SE5;
GN   OrderedLocusNames=Os06g0603000, LOC_Os06g40080;
GN   ORFNames=OsJ_21897, P0486H12.31;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Xu S., Wu T.T., Lu H., Ling T.F., Xuan W., Sun Y.G., Cao Z., Shen W.B.;
RT   "Cloning and characterization of heme oxygenase-1 from Oryza sativa.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10849355; DOI=10.1046/j.1365-313x.2000.00753.x;
RA   Izawa T., Oikawa T., Tokutomi S., Okuno K., Shimamoto K.;
RT   "Phytochromes confer the photoperiodic control of flowering in rice (a
RT   short-day plant).";
RL   Plant J. 22:391-399(2000).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19675157; DOI=10.1104/pp.109.139097;
RA   Andres F., Galbraith D.W., Talon M., Domingo C.;
RT   "Analysis of PHOTOPERIOD SENSITIVITY5 sheds light on the role of
RT   phytochromes in photoperiodic flowering in rice.";
RL   Plant Physiol. 151:681-690(2009).
CC   -!- FUNCTION: Catalyzes the opening of the heme ring to form the open-chain
CC       tetrapyrrole biliverdin IX with the release of iron and carbon monoxide
CC       (CO). Is a key enzyme in the synthesis of the chromophore of the
CC       phytochrome family of plant photoreceptors. Essential for photoperiod
CC       response and repression of flowering through cytochromes that inhibit
CC       flowering by affecting both HD1 and EHD1 flowering pathways.
CC       {ECO:0000269|PubMed:10849355, ECO:0000269|PubMed:19675157}.
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 [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:60344; EC=1.14.14.18;
CC         Evidence={ECO:0000250|UniProtKB:O48782};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DISRUPTION PHENOTYPE: Pale green and very early flowering phenotype and
CC       complete deficiency in photoperiodic response. Lack of photoreversible
CC       phytochromes and responses of coleoptile elongation by light pulses.
CC       {ECO:0000269|PubMed:10849355, ECO:0000269|PubMed:19675157}.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR   EMBL; EU781632; ACE98543.1; -; mRNA.
DR   EMBL; AP003615; BAD35463.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF19925.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS98507.1; -; Genomic_DNA.
DR   EMBL; CM000143; EEE65978.1; -; Genomic_DNA.
DR   EMBL; AK068856; BAG91127.1; -; mRNA.
DR   EMBL; AK104955; BAG97040.1; -; mRNA.
DR   RefSeq; XP_015643881.1; XM_015788395.1.
DR   AlphaFoldDB; Q69XJ4; -.
DR   SMR; Q69XJ4; -.
DR   STRING; 4530.OS06T0603000-01; -.
DR   PaxDb; Q69XJ4; -.
DR   PRIDE; Q69XJ4; -.
DR   EnsemblPlants; Os06t0603000-01; Os06t0603000-01; Os06g0603000.
DR   GeneID; 4341462; -.
DR   Gramene; Os06t0603000-01; Os06t0603000-01; Os06g0603000.
DR   KEGG; osa:4341462; -.
DR   eggNOG; KOG4480; Eukaryota.
DR   HOGENOM; CLU_063325_1_0_1; -.
DR   InParanoid; Q69XJ4; -.
DR   OMA; PPEFICH; -.
DR   OrthoDB; 1408918at2759; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000007752; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q69XJ4; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; ISS:Gramene.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006788; P:heme oxidation; ISS:Gramene.
DR   GO; GO:0010229; P:inflorescence development; IMP:Gramene.
DR   GO; GO:0009648; P:photoperiodism; IMP:Gramene.
DR   GO; GO:0048573; P:photoperiodism, flowering; IMP:UniProtKB.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd19165; HemeO; 1.
DR   Gene3D; 1.20.910.10; -; 1.
DR   InterPro; IPR002051; Haem_Oase.
DR   InterPro; IPR016053; Haem_Oase-like.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR016951; Haem_Oase_decyc_pln.
DR   PANTHER; PTHR35703; PTHR35703; 1.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   PIRSF; PIRSF030219; Heme_Oase_decyc_pln; 1.
DR   SUPFAM; SSF48613; SSF48613; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Heme; Iron; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..64
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           65..289
FT                   /note="Heme oxygenase 1, chloroplastic"
FT                   /id="PRO_0000412189"
FT   BINDING         96
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   289 AA;  31918 MW;  C03B0103AD2E6E91 CRC64;
     MAPAAASLTA PNALAATSLP FLHGRKSGGG GVSVHAGAPS PSRAVAVVAR RLWGSASSSR
     RMVVAAATAA EMAPAASGEE GKPFVEEMRA VAMRLHTKDQ AKEGEKEPQA PPVARWEPSV
     DGYLRFLVDS KLVFETLETI VDRAAVPWYA EFRNTGLERS EQLKKDLEWF KEQGHTIPEP
     SAPGTTYASY LEELAEKDSQ AFICHFYNVY FAHTAGGRMI GKKVSENILN KKELEFYKWE
     GNLSQLLQNV RNKLNEVASS WTREEKDHCL DETEKSFSYS GDLLRHIFT