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Protein

Heme oxygenase 4, chloroplastic

Gene

HO4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.2 Publications

Catalytic activityi

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

pH dependencei

Optimum pH is 7.2.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Iron (heme axial ligand)By similarity

GO - Molecular functioni

  • heme binding Source: TAIR
  • heme oxygenase (decyclizing) activity Source: TAIR
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Photosynthesis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT1G58300-MONOMER.
MetaCyc:AT1G58300-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 4, chloroplastic (EC:1.14.99.3)
Gene namesi
Name:HO4
Ordered Locus Names:At1g58300
ORF Names:F19C14.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G58300.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 283Heme oxygenase 4, chloroplasticPRO_0000412188
Transit peptidei1 – ?ChloroplastSequence Analysis

Expressioni

Tissue specificityi

Widely expressed at low levels.1 Publication

Gene expression databases

GenevestigatoriQ9LQC0.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G58300.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9LQC0.
SMRiQ9LQC0. Positions 78-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG255302.
HOGENOMiHOG000265822.
InParanoidiQ9LQC0.
KOiK00510.
OMAiYNINFAH.
PhylomeDBiQ9LQC0.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR016951. Haem_Oase_decyc_pln.
[Graphical view]
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF030219. Heme_Oase_decyc_pln. 1 hit.
SUPFAMiSSF48613. SSF48613. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LQC0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSRLNASC RFPASRRLDC ESYVSLRAKT VTIRYVRTIA APRRHLVRRA
60 70 80 90 100
NEDQTLVVNV VAAAGEKPER RYPREPNGFV EEMRFVVMKI HPRDQVKEGK
110 120 130 140 150
SDSNDLVSTW NFTIEGYLKF LVDSKLVFET LERIINESAI QAYAGLKNTG
160 170 180 190 200
LERAENLSRD LEWFKEQGYE IPESMVPGKA YSQYLKNIAE KDPPAFICHF
210 220 230 240 250
YNINFAHSAG GRMIGTKVAE KILDNKELEF YKWDGQLSEL LQNVSEELNK
260 270 280
VAELWTREEK NHCLEETEKS FKFYWEIFRY LLS
Length:283
Mass (Da):32,953
Last modified:October 1, 2000 - v1
Checksum:iAB44816340D77DF5
GO

Sequence cautioni

The sequence ABK28442.1 differs from that shown. Reason: Erroneous termination at position 284. Translated as stop.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 943PRD → QEI in AAK63007 (PubMed:11402195).Curated
Sequence conflicti102 – 1021D → V in AAK63007 (PubMed:11402195).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320023 Genomic DNA. Translation: AAK63007.1.
AC008051 Genomic DNA. Translation: AAF82257.1.
CP002684 Genomic DNA. Translation: AEE33533.1.
DQ446372 mRNA. Translation: ABE65721.1.
DQ652902 mRNA. Translation: ABK28442.1. Sequence problems.
AF295364 Genomic DNA. Translation: AAG30207.1.
PIRiF96616.
RefSeqiNP_176126.1. NM_104610.1.
UniGeneiAt.52255.

Genome annotation databases

EnsemblPlantsiAT1G58300.1; AT1G58300.1; AT1G58300.
GeneIDi842199.
KEGGiath:AT1G58300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320023 Genomic DNA. Translation: AAK63007.1.
AC008051 Genomic DNA. Translation: AAF82257.1.
CP002684 Genomic DNA. Translation: AEE33533.1.
DQ446372 mRNA. Translation: ABE65721.1.
DQ652902 mRNA. Translation: ABK28442.1. Sequence problems.
AF295364 Genomic DNA. Translation: AAG30207.1.
PIRiF96616.
RefSeqiNP_176126.1. NM_104610.1.
UniGeneiAt.52255.

3D structure databases

ProteinModelPortaliQ9LQC0.
SMRiQ9LQC0. Positions 78-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G58300.1-P.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G58300.1; AT1G58300.1; AT1G58300.
GeneIDi842199.
KEGGiath:AT1G58300.

Organism-specific databases

TAIRiAT1G58300.

Phylogenomic databases

eggNOGiNOG255302.
HOGENOMiHOG000265822.
InParanoidiQ9LQC0.
KOiK00510.
OMAiYNINFAH.
PhylomeDBiQ9LQC0.

Enzyme and pathway databases

BioCyciARA:AT1G58300-MONOMER.
MetaCyc:AT1G58300-MONOMER.

Miscellaneous databases

PROiQ9LQC0.

Gene expression databases

GenevestigatoriQ9LQC0.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR016951. Haem_Oase_decyc_pln.
[Graphical view]
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF030219. Heme_Oase_decyc_pln. 1 hit.
SUPFAMiSSF48613. SSF48613. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The heme-oxygenase family required for phytochrome chromophore biosynthesis is necessary for proper photomorphogenesis in higher plants."
    Davis S.J., Bhoo S.H., Durski A.M., Walker J.M., Vierstra R.D.
    Plant Physiol. 126:656-669(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
    Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
    Plant Biotechnol. J. 4:317-324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Regulation of HEMA1 expression by phytochrome and a plastid signal during de-etiolation in Arabidopsis thaliana."
    McCormac A.C., Fischer A., Kumar A.M., Soll D., Terry M.J.
    Plant J. 25:549-561(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-283.
  6. "Multiple heme oxygenase family members contribute to the biosynthesis of the phytochrome chromophore in Arabidopsis."
    Emborg T.J., Walker J.M., Noh B., Vierstra R.D.
    Plant Physiol. 140:856-868(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  7. "Characterization of the haem oxygenase protein family in Arabidopsis thaliana reveals a diversity of functions."
    Gisk B., Yasui Y., Kohchi T., Frankenberg-Dinkel N.
    Biochem. J. 425:425-434(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiHMOX4_ARATH
AccessioniPrimary (citable) accession number: Q9LQC0
Secondary accession number(s): A0MED2, Q94FX2, Q9FUN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.