HMOX1_ARATH
ID HMOX1_ARATH Reviewed; 282 AA.
AC O48782; B3H4A6; Q7E9A5; Q9FPE3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Heme oxygenase 1, chloroplastic;
DE Short=AtHO1;
DE EC=1.14.14.18 {ECO:0000269|PubMed:10072395, ECO:0000269|PubMed:12481078};
DE AltName: Full=Protein GENOMES UNCOUPLED 2;
DE AltName: Full=Protein REVERSAL OF THE DET PHENOTYPE 4;
DE Flags: Precursor;
GN Name=HO1; Synonyms=GUN2, HY1, HY6, TED4; OrderedLocusNames=At2g26670;
GN ORFNames=F18A8.4;
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 / MRNA] (ISOFORM 1), FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10072395; DOI=10.2307/3870864;
RA Muramoto T., Kohchi T., Yokota A., Hwang I., Goodman H.M.;
RT "The Arabidopsis photomorphogenic mutant hy1 is deficient in phytochrome
RT chromophore biosynthesis as a result of a mutation in a plastid heme
RT oxygenase.";
RL Plant Cell 11:335-348(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
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 [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=12359912; DOI=10.2307/3868934;
RA Chory J., Peto C.A., Ashbaugh M., Saganich R., Pratt L., Ausubel F.;
RT "Different roles for phytochrome in etiolated and green plants deduced from
RT characterization of Arabidopsis thaliana mutants.";
RL Plant Cell 1:867-880(1989).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12324588; DOI=10.2307/3869225;
RA Parks B.M., Quail P.H.;
RT "Phytochrome-deficient hy1 and hy2 long hypocotyl mutants of Arabidopsis
RT are defective in phytochrome chromophore biosynthesis.";
RL Plant Cell 3:1177-1186(1991).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7690685; DOI=10.1016/0092-8674(93)90459-4;
RA Susek R.E., Ausubel F.M., Chory J.;
RT "Signal transduction mutants of Arabidopsis uncouple nuclear CAB and RBCS
RT gene expression from chloroplast development.";
RL Cell 74:787-799(1993).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12232145; DOI=10.1104/pp.104.3.1027;
RA Neff M.M., Van Volkenburgh E.;
RT "Light-stimulated cotyledon expansion in Arabidopsis seedlings (the role of
RT phytochrome b).";
RL Plant Physiol. 104:1027-1032(1994).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11135121; DOI=10.1046/j.1365-313x.2000.00936.x;
RA Vinti G., Hills A., Campbell S., Bowyer J.R., Mochizuki N., Chory J.,
RA Lopez-Juez E.;
RT "Interactions between hy1 and gun mutants of Arabidopsis, and their
RT implications for plastid/nuclear signalling.";
RL Plant J. 24:883-894(2000).
RN [12]
RP FUNCTION.
RX PubMed=11172074; DOI=10.1073/pnas.98.4.2053;
RA Mochizuki N., Brusslan J.A., Larkin R., Nagatani A., Chory J.;
RT "Arabidopsis genomes uncoupled 5 (GUN5) mutant reveals the involvement of
RT Mg-chelatase H subunit in plastid-to-nucleus signal transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2053-2058(2001).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12481078; DOI=10.1104/pp.008128;
RA Muramoto T., Tsurui N., Terry M.J., Yokota A., Kohchi T.;
RT "Expression and biochemical properties of a ferredoxin-dependent heme
RT oxygenase required for phytochrome chromophore synthesis.";
RL Plant Physiol. 130:1958-1966(2002).
RN [14]
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 [15]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17567636; DOI=10.1093/pcp/pcm076;
RA Zhai Q., Li C.B., Zheng W., Wu X., Zhao J., Zhou G., Jiang H., Sun J.,
RA Lou Y., Li C.;
RT "Phytochrome chromophore deficiency leads to overproduction of jasmonic
RT acid and elevated expression of jasmonate-responsive genes in
RT Arabidopsis.";
RL Plant Cell Physiol. 48:1061-1071(2007).
RN [16]
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).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20979354; DOI=10.1021/bi1014369;
RA Gisk B., Bregier F., Krueger R.A., Broering M., Frankenberg-Dinkel N.;
RT "Enzymatic ring opening of an iron corrole by plant-type heme oxygenases:
RT unexpected substrate and protein selectivities.";
RL Biochemistry 49:10042-10044(2010).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21205037; DOI=10.1111/j.1365-313x.2011.04488.x;
RA Xie Y.J., Xu S., Han B., Wu M.Z., Yuan X.X., Han Y., Gu Q., Xu D.K.,
RA Yang Q., Shen W.B.;
RT "Evidence of Arabidopsis salt acclimation induced by up-regulation of HY1
RT and the regulatory role of RbohD-derived reactive oxygen species
RT synthesis.";
RL Plant J. 66:280-292(2011).
CC -!- FUNCTION: Key enzyme in the synthesis of the chromophore of the
CC phytochrome family of plant photoreceptors. Catalyzes the opening of
CC the heme ring to form the open-chain tetrapyrrole biliverdin IX with
CC the release of iron and carbon monoxide (CO). Produces specifically the
CC biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-
CC dependent and its activity is increased in the presence of ascorbate.
CC Plays a role in salt acclimation signaling. May affect the plastid-to-
CC nucleus signaling pathway by perturbing tetrapyrrole synthesis. The
CC plastid-to-nucleus signal plays an important role in the coordinated
CC expression of both nuclear- and chloroplast-localized genes that encode
CC photosynthesis-related proteins. {ECO:0000269|PubMed:10072395,
CC ECO:0000269|PubMed:10339624, ECO:0000269|PubMed:11135121,
CC ECO:0000269|PubMed:11172074, ECO:0000269|PubMed:12232145,
CC ECO:0000269|PubMed:12324588, ECO:0000269|PubMed:12481078,
CC ECO:0000269|PubMed:16428602, ECO:0000269|PubMed:19860740,
CC ECO:0000269|PubMed:20979354, ECO:0000269|PubMed:21205037,
CC ECO:0000269|PubMed:7690685}.
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:0000269|PubMed:10072395, ECO:0000269|PubMed:12481078};
CC -!- ACTIVITY REGULATION: Activated by ascorbate.
CC {ECO:0000269|PubMed:12481078}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for hemin {ECO:0000269|PubMed:12481078,
CC ECO:0000269|PubMed:19860740};
CC KM=1.9 uM for ferredoxin {ECO:0000269|PubMed:12481078,
CC ECO:0000269|PubMed:19860740};
CC KM=420 uM for ascorbate {ECO:0000269|PubMed:12481078,
CC ECO:0000269|PubMed:19860740};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:12481078,
CC ECO:0000269|PubMed:19860740};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10072395, ECO:0000269|PubMed:19860740}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O48782-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O48782-2; Sequence=VSP_041652;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10339624,
CC ECO:0000269|PubMed:16428602, ECO:0000269|PubMed:20979354}.
CC -!- INDUCTION: By salt treatment. Down-regulated by jasmonate.
CC {ECO:0000269|PubMed:17567636, ECO:0000269|PubMed:20979354}.
CC -!- DISRUPTION PHENOTYPE: Long hypocotyl, incomplete chloroplast and leaf
CC development, lack of photoreversible phytochromes and lack of
CC phytochromobilin, the phytochrome chromophore. No cotyledon expansion
CC in response to bright-red light. Increased levels of jasmonate (JA) and
CC constitutive expression of JA-inducible defense genes. Increased
CC sensitivity to salt stress and no acclimation response to salinity.
CC {ECO:0000269|PubMed:10072395, ECO:0000269|PubMed:10339624,
CC ECO:0000269|PubMed:11135121, ECO:0000269|PubMed:12232145,
CC ECO:0000269|PubMed:12324588, ECO:0000269|PubMed:12359912,
CC ECO:0000269|PubMed:16428602, ECO:0000269|PubMed:17567636,
CC ECO:0000269|PubMed:20979354, ECO:0000269|PubMed:21205037,
CC ECO:0000269|PubMed:7690685}.
CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK52998.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB021857; BAA77758.1; -; Genomic_DNA.
DR EMBL; AB021858; BAA77759.1; -; mRNA.
DR EMBL; AF132475; AAD22107.1; -; Genomic_DNA.
DR EMBL; AF132476; AAD22108.1; -; Genomic_DNA.
DR EMBL; AC003105; AAB95301.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07872.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07873.1; -; Genomic_DNA.
DR EMBL; AF327418; AAG42008.2; -; mRNA.
DR EMBL; AF375414; AAK52998.1; ALT_INIT; mRNA.
DR EMBL; AY129477; AAM91063.1; -; mRNA.
DR EMBL; BT002327; AAN86160.1; -; mRNA.
DR EMBL; AY087288; AAM64841.1; -; mRNA.
DR PIR; T52457; T52457.
DR RefSeq; NP_001118392.1; NM_001124920.1. [O48782-2]
DR RefSeq; NP_180235.1; NM_128224.3. [O48782-1]
DR AlphaFoldDB; O48782; -.
DR SMR; O48782; -.
DR BioGRID; 2560; 1.
DR STRING; 3702.AT2G26670.1; -.
DR iPTMnet; O48782; -.
DR PaxDb; O48782; -.
DR PRIDE; O48782; -.
DR ProteomicsDB; 232086; -. [O48782-1]
DR EnsemblPlants; AT2G26670.1; AT2G26670.1; AT2G26670. [O48782-1]
DR EnsemblPlants; AT2G26670.2; AT2G26670.2; AT2G26670. [O48782-2]
DR GeneID; 817208; -.
DR Gramene; AT2G26670.1; AT2G26670.1; AT2G26670. [O48782-1]
DR Gramene; AT2G26670.2; AT2G26670.2; AT2G26670. [O48782-2]
DR KEGG; ath:AT2G26670; -.
DR Araport; AT2G26670; -.
DR TAIR; locus:2005513; AT2G26670.
DR eggNOG; KOG4480; Eukaryota.
DR HOGENOM; CLU_063325_1_1_1; -.
DR InParanoid; O48782; -.
DR OMA; PPEFICH; -.
DR PhylomeDB; O48782; -.
DR BioCyc; ARA:AT2G26670-MON; -.
DR BioCyc; MetaCyc:AT2G26670-MON; -.
DR PRO; PR:O48782; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48782; baseline and differential.
DR Genevisible; O48782; 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:0016117; P:carotenoid biosynthetic process; IMP:TAIR.
DR GO; GO:0071494; P:cellular response to UV-C; IMP:TAIR.
DR GO; GO:0010019; P:chloroplast-nucleus signaling pathway; IMP:TAIR.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IMP:TAIR.
DR GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0010024; P:phytochromobilin biosynthetic process; IDA:TAIR.
DR GO; GO:0010075; P:regulation of meristem growth; IGI:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IGI:TAIR.
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..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..282
FT /note="Heme oxygenase 1, chloroplastic"
FT /id="PRO_0000412185"
FT BINDING 86
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 94..142
FT /note="GEKETKSIEERPVAKWEPTVEGYLRFLVDSKLVYDTLELIIQDSNFPTY ->
FT D (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041652"
SQ SEQUENCE 282 AA; 32691 MW; 65D9638890A3E8BA CRC64;
MAYLAPISSS LSIFKNPQLS RFQFSSSSPN PLFLRPRIQI LSMTMNKSPS LVVVAATTAA
EKQKKRYPGE SKGFVEEMRF VAMRLHTKDQ AKEGEKETKS IEERPVAKWE PTVEGYLRFL
VDSKLVYDTL ELIIQDSNFP TYAEFKNTGL ERAEKLSTDL EWFKEQGYEI PEPTAPGKTY
SQYLKELAEK DPQAFICHFY NIYFAHSAGG RMIGRKVAER ILDNKELEFY KWDGELSQLL
QNVREKLNKV AEEWTREEKN HCLEETEKSF KYSGEILRLI LS
