ID   HMOX2_ARATH             Reviewed;         299 AA.
AC   O48722;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Probable inactive heme oxygenase 2, chloroplastic;
DE            Short=AtHO2;
DE   Flags: Precursor;
GN   Name=HO2; OrderedLocusNames=At2g26550; ORFNames=T9J22.22;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10339624; DOI=10.1073/pnas.96.11.6541;
RA   Davis S.J., Kurepa J., Vierstra R.D.;
RT   "The Arabidopsis thaliana HY1 locus, required for phytochrome-chromophore
RT   biosynthesis, encodes a protein related to heme oxygenases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:6541-6546(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16428602; DOI=10.1104/pp.105.074211;
RA   Emborg T.J., Walker J.M., Noh B., Vierstra R.D.;
RT   "Multiple heme oxygenase family members contribute to the biosynthesis of
RT   the phytochrome chromophore in Arabidopsis.";
RL   Plant Physiol. 140:856-868(2006).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19860740; DOI=10.1042/bj20090775;
RA   Gisk B., Yasui Y., Kohchi T., Frankenberg-Dinkel N.;
RT   "Characterization of the haem oxygenase protein family in Arabidopsis
RT   thaliana reveals a diversity of functions.";
RL   Biochem. J. 425:425-434(2010).
CC   -!- FUNCTION: Probable inactive heme oxygenase. Binds protoporphyrin IX, a
CC       precursor for both heme and chlorophyll biosynthesis. Plays a minor
CC       role in phytochrome assembly and photomorphogenesis.
CC       {ECO:0000269|PubMed:16428602, ECO:0000269|PubMed:19860740}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:19860740}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O48722-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Widely expressed at low levels.
CC       {ECO:0000269|PubMed:16428602}.
CC   -!- DISRUPTION PHENOTYPE: Slight reduction in plant size and chlorophyll
CC       content, and early flowering. {ECO:0000269|PubMed:16428602}.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved His residue involved in heme iron binding
CC       and essential for heme oxygenase activity. Its enzyme activity is
CC       therefore unsure. {ECO:0000305}.
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DR   EMBL; AF132477; AAD22109.1; -; Genomic_DNA.
DR   EMBL; AC002505; AAC14503.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07856.1; -; Genomic_DNA.
DR   PIR; H84661; H84661.
DR   PIR; T00988; T00988.
DR   RefSeq; NP_001189610.1; NM_001202681.2. [O48722-1]
DR   AlphaFoldDB; O48722; -.
DR   SMR; O48722; -.
DR   iPTMnet; O48722; -.
DR   PRIDE; O48722; -.
DR   ProteomicsDB; 230211; -. [O48722-1]
DR   EnsemblPlants; AT2G26550.2; AT2G26550.2; AT2G26550. [O48722-1]
DR   GeneID; 817196; -.
DR   Gramene; AT2G26550.2; AT2G26550.2; AT2G26550. [O48722-1]
DR   KEGG; ath:AT2G26550; -.
DR   Araport; AT2G26550; -.
DR   HOGENOM; CLU_063325_0_0_1; -.
DR   InParanoid; O48722; -.
DR   PhylomeDB; O48722; -.
DR   PRO; PR:O48722; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O48722; baseline and differential.
DR   Genevisible; O48722; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:InterPro.
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; -; 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   Alternative splicing; Chloroplast; Photosynthesis; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..83
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           84..299
FT                   /note="Probable inactive heme oxygenase 2, chloroplastic"
FT                   /id="PRO_0000412186"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..122
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   299 AA;  34902 MW;  B7CEDF24520A437E CRC64;
     MASLLRPTPL LSTPRKLTHS HLHTSISFPF QISTQRKPQK HLLNLCRSTP TPSQQKASQR
     KRTRYRKQYP GENIGITEEM RFVAMRLRNV NGKKLDLSED KTDTEKEEEE EEEDDDDDDE
     VKEETWKPSK EGFLKYLVDS KLVFDTIERI VDESENVSYA YFRRTGLERC ESIEKDLQWL
     REQDLVIPEP SNVGVSYAKY LEEQAGESAP LFLSHFYSIY FSHIAGGQVL VRQVSEKLLE
     GKELEFNRWE GDAQDLLKGV REKLNVLGEH WSRDEKNKCL KETAKAFKYM GQIVRLIIL