HMOX3_ARATH
ID HMOX3_ARATH Reviewed; 285 AA.
AC Q9C9L4; B3H531;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Heme oxygenase 3, chloroplastic;
DE EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
DE Flags: Precursor;
GN Name=HO3; OrderedLocusNames=At1g69720; ORFNames=T6C23.8;
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] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:19860740};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19860740}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C9L4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C9L4-2; Sequence=VSP_041653, VSP_041654;
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}.
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DR EMBL; AF320022; AAK63006.1; -; Genomic_DNA.
DR EMBL; AC013289; AAG52552.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34966.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34967.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59442.1; -; Genomic_DNA.
DR EMBL; AY084250; AAM60844.1; -; mRNA.
DR PIR; B96719; B96719.
DR RefSeq; NP_001117574.1; NM_001124102.1. [Q9C9L4-2]
DR RefSeq; NP_001321799.1; NM_001334420.1. [Q9C9L4-1]
DR RefSeq; NP_177130.1; NM_105640.4. [Q9C9L4-1]
DR AlphaFoldDB; Q9C9L4; -.
DR SMR; Q9C9L4; -.
DR STRING; 3702.AT1G69720.1; -.
DR PaxDb; Q9C9L4; -.
DR PRIDE; Q9C9L4; -.
DR ProteomicsDB; 232100; -. [Q9C9L4-1]
DR EnsemblPlants; AT1G69720.1; AT1G69720.1; AT1G69720. [Q9C9L4-1]
DR EnsemblPlants; AT1G69720.2; AT1G69720.2; AT1G69720. [Q9C9L4-2]
DR EnsemblPlants; AT1G69720.3; AT1G69720.3; AT1G69720. [Q9C9L4-1]
DR GeneID; 843308; -.
DR Gramene; AT1G69720.1; AT1G69720.1; AT1G69720. [Q9C9L4-1]
DR Gramene; AT1G69720.2; AT1G69720.2; AT1G69720. [Q9C9L4-2]
DR Gramene; AT1G69720.3; AT1G69720.3; AT1G69720. [Q9C9L4-1]
DR KEGG; ath:AT1G69720; -.
DR Araport; AT1G69720; -.
DR TAIR; locus:2205045; AT1G69720.
DR eggNOG; KOG4480; Eukaryota.
DR HOGENOM; CLU_063325_1_1_1; -.
DR InParanoid; Q9C9L4; -.
DR OMA; GQPVAKW; -.
DR OrthoDB; 1408918at2759; -.
DR PhylomeDB; Q9C9L4; -.
DR BioCyc; ARA:AT1G69720-MON; -.
DR BioCyc; MetaCyc:AT1G69720-MON; -.
DR PRO; PR:Q9C9L4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9L4; baseline and differential.
DR Genevisible; Q9C9L4; AT.
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: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 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Heme; Iron; Metal-binding;
KW Oxidoreductase; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..285
FT /note="Heme oxygenase 3, chloroplastic"
FT /id="PRO_0000412187"
FT REGION 89..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89
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 VAR_SEQ 220..227
FT /note="VSKKILDN -> LCRYLRRY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041653"
FT VAR_SEQ 228..285
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041654"
SQ SEQUENCE 285 AA; 32434 MW; D552E638E7DFF241 CRC64;
MATTRLNPSC HFPASTRLSC ESYLGLRTTG RISYARTLTA PRGYLAVKAN GGQASVVTAA
AITEKQQKKY PGESKGFVEE MRFVAMRLHT KDQAREGEKE SRSPEEGPVA KWEPTVEGYL
HFLVDSKLVY DTLEGIIDGS NFPTYAGFKN TGLERAESLR KDLEWFKEQG YEIPEPMAPG
KTYSEYLKDL AENDPQAFIC HFYNIYFAHS AGGQMIGTKV SKKILDNKEL EFYKWDGQLS
QLLQNVRQKL NKVAEWWTRE EKSHCLEETE KSFKFSGEIL RLILS
