ID   HMOX4_ARATH             Reviewed;         283 AA.
AC   Q9LQC0; A0MED2; Q94FX2; Q9FUN4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=Heme oxygenase 4, chloroplastic;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
DE   Flags: Precursor;
GN   Name=HO4; OrderedLocusNames=At1g58300; ORFNames=F19C14.8;
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=11402195; DOI=10.1104/pp.126.2.656;
RA   Davis S.J., Bhoo S.H., Durski A.M., Walker J.M., Vierstra R.D.;
RT   "The heme-oxygenase family required for phytochrome chromophore
RT   biosynthesis is necessary for proper photomorphogenesis in higher plants.";
RL   Plant Physiol. 126:656-669(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 144-283.
RX   PubMed=11309145; DOI=10.1046/j.1365-313x.2001.00986.x;
RA   McCormac A.C., Fischer A., Kumar A.M., Soll D., Terry M.J.;
RT   "Regulation of HEMA1 expression by phytochrome and a plastid signal during
RT   de-etiolation in Arabidopsis thaliana.";
RL   Plant J. 25:549-561(2001).
RN   [6]
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   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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: 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). Produces specifically the biliverdin IX-alpha isomer. Plays a
CC       minor role in phytochrome assembly and photomorphogenesis.
CC       {ECO:0000269|PubMed:16428602, ECO:0000269|PubMed:19860740}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.2. {ECO:0000269|PubMed:19860740};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:19860740}.
CC   -!- TISSUE SPECIFICITY: Widely expressed at low levels.
CC       {ECO:0000269|PubMed:16428602}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:16428602}.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28442.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF320023; AAK63007.1; -; Genomic_DNA.
DR   EMBL; AC008051; AAF82257.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33533.1; -; Genomic_DNA.
DR   EMBL; DQ446372; ABE65721.1; -; mRNA.
DR   EMBL; DQ652902; ABK28442.1; ALT_SEQ; mRNA.
DR   EMBL; AF295364; AAG30207.1; -; Genomic_DNA.
DR   PIR; F96616; F96616.
DR   RefSeq; NP_176126.1; NM_104610.2.
DR   AlphaFoldDB; Q9LQC0; -.
DR   SMR; Q9LQC0; -.
DR   STRING; 3702.Q9LQC0; -.
DR   PaxDb; 3702-AT1G58300-1; -.
DR   ProteomicsDB; 230212; -.
DR   EnsemblPlants; AT1G58300.1; AT1G58300.1; AT1G58300.
DR   GeneID; 842199; -.
DR   Gramene; AT1G58300.1; AT1G58300.1; AT1G58300.
DR   KEGG; ath:AT1G58300; -.
DR   Araport; AT1G58300; -.
DR   TAIR; AT1G58300; HO4.
DR   eggNOG; KOG4480; Eukaryota.
DR   HOGENOM; CLU_063325_1_1_1; -.
DR   InParanoid; Q9LQC0; -.
DR   OMA; HFYNINF; -.
DR   OrthoDB; 654527at2759; -.
DR   PhylomeDB; Q9LQC0; -.
DR   BioCyc; ARA:AT1G58300-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G58300-MONOMER; -.
DR   PRO; PR:Q9LQC0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LQC0; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0020037; F:heme binding; IDA:TAIR.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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; IPR016951; Haem_Oase_decyc_pln.
DR   PANTHER; PTHR35703; HEME OXYGENASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR35703:SF2; HEME OXYGENASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   PIRSF; PIRSF030219; Heme_Oase_decyc_pln; 1.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR   Genevisible; Q9LQC0; AT.
PE   1: Evidence at protein level;
KW   Chloroplast; Heme; Iron; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..283
FT                   /note="Heme oxygenase 4, chloroplastic"
FT                   /id="PRO_0000412188"
FT   BINDING         91
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"
FT   CONFLICT        92..94
FT                   /note="PRD -> QEI (in Ref. 1; AAK63007)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="D -> V (in Ref. 1; AAK63007)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   283 AA;  32953 MW;  AB44816340D77DF5 CRC64;
     MATSRLNASC RFPASRRLDC ESYVSLRAKT VTIRYVRTIA APRRHLVRRA NEDQTLVVNV
     VAAAGEKPER RYPREPNGFV EEMRFVVMKI HPRDQVKEGK SDSNDLVSTW NFTIEGYLKF
     LVDSKLVFET LERIINESAI QAYAGLKNTG LERAENLSRD LEWFKEQGYE IPESMVPGKA
     YSQYLKNIAE KDPPAFICHF YNINFAHSAG GRMIGTKVAE KILDNKELEF YKWDGQLSEL
     LQNVSEELNK VAELWTREEK NHCLEETEKS FKFYWEIFRY LLS
//