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Protein

Peroxisomal (S)-2-hydroxy-acid oxidase GLO1

Gene

GLO1

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Photorespiratory enzyme that can exert a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase. Not required for oxalate accumulation.2 Publications

Catalytic activityi

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.1 Publication

Cofactori

FMNPROSITE-ProRule annotation

Kineticsi

  1. KM=0.4 mM for glycolate (at pH 8.0 and 30 degrees Celsius)1 Publication
  2. KM=4 mM for glyoxylate (at pH 8.0 and 30 degrees Celsius)1 Publication

    Pathway:iphotorespiration

    This protein is involved in step 2 of the subpathway that synthesizes glycine from 2-phosphoglycolate.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Peroxisomal (S)-2-hydroxy-acid oxidase GLO4 (GLO4), Peroxisomal (S)-2-hydroxy-acid oxidase GLO1 (GLO1), Peroxisomal (S)-2-hydroxy-acid oxidase GLO5 (GLO5), Peroxisomal (S)-2-hydroxy-acid oxidase GLO2 (GLO2), Peroxisomal (S)-2-hydroxy-acid oxidase GLO3 (GLO3)
    3. no protein annotated in this organism
    This subpathway is part of the pathway photorespiration, which is itself part of Photosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from 2-phosphoglycolate, the pathway photorespiration and in Photosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei25 – 251SubstratePROSITE-ProRule annotation
    Binding sitei107 – 1071FMNPROSITE-ProRule annotation
    Binding sitei128 – 1281FMNPROSITE-ProRule annotation
    Binding sitei130 – 1301SubstratePROSITE-ProRule annotation
    Binding sitei156 – 1561FMNPROSITE-ProRule annotation
    Binding sitei165 – 1651SubstratePROSITE-ProRule annotation
    Binding sitei231 – 2311FMNPROSITE-ProRule annotation
    Active sitei255 – 2551Proton acceptorPROSITE-ProRule annotation
    Binding sitei258 – 2581SubstratePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi286 – 31025FMNPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    • modulation by virus of host morphology or physiology Source: UniProtKB
    • oxidative photosynthetic carbon pathway Source: UniProtKB-UniPathway
    • photorespiration Source: UniProtKB
    • regulation of photosynthesis Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolate pathway, Host-virus interaction, Photorespiration

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BRENDAi1.1.3.15. 4460.
    ReactomeiREACT_272074. Glyoxylate metabolism.
    UniPathwayiUPA00951; UER00912.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal (S)-2-hydroxy-acid oxidase GLO1 (EC:1.1.3.15)
    Alternative name(s):
    Glycolate oxidase 1
    Short name:
    GOX 1
    Short name:
    OsGLO1
    Short chain alpha-hydroxy acid oxidase GLO1
    Gene namesi
    Name:GLO1
    Synonyms:GOX
    Ordered Locus Names:Os03g0786100, LOC_Os03g57220
    ORF Names:OsJ_12861
    OrganismiOryza sativa subsp. japonica (Rice)
    Taxonomic identifieri39947 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
    ProteomesiUP000000763 Componenti: Chromosome 3

    Organism-specific databases

    GrameneiQ10CE4.

    Subcellular locationi

    • Peroxisome 1 Publication

    GO - Cellular componenti

    • peroxisome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 369369Peroxisomal (S)-2-hydroxy-acid oxidase GLO1PRO_0000403409Add
    BLAST

    Proteomic databases

    PaxDbiQ10CE4.

    Expressioni

    Tissue specificityi

    Expressed constitutively in leaves (at protein level).1 Publication

    Interactioni

    Subunit structurei

    Homotetramer or homooctamer (By similarity). Interacts with rice dwarf virus (RDV) P8. This interaction promotes viral P8 relocation to virus factories peripheral to peroxisomes.By similarity1 Publication

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g57220.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ10CE4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 360360FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi367 – 3693Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
    Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1304.
    InParanoidiQ10CE4.
    KOiK11517.
    OMAiITSAMVV.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view]
    PfamiPF01070. FMN_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q10CE4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGEITNVMEY QAIAKQKLPK MIYDYYASGA EDEWTLKENR EAFSRILFRP
    60 70 80 90 100
    RILIDVSKID MSATVLGFKI SMPIMIAPSA MQKMAHPDGE YATARAASAA
    110 120 130 140 150
    GTIMTLSSWA TSSVEEVAST GPGIRFFQLY VYKDRNVVEQ LVRRAERAGF
    160 170 180 190 200
    KAIALTVDTP RLGRREADIK NRFVLPPYLT LKNFEGLDLA EMDKSNDSGL
    210 220 230 240 250
    ASYVAGQIDR TLSWKDVKWL QSITSLPILV KGVITAEDAR LAVHSGAAGI
    260 270 280 290 300
    IVSNHGARQL DYVPATISAL EEVVTAAAGR IPVYLDGGVR RGTDVFKALA
    310 320 330 340 350
    LGAAGVFIGR PVVFALAAEG EAGVRNVLRM MREEFELTMA LSGCTSLADI
    360
    TRAHIYTDAD RLARPFPRL
    Length:369
    Mass (Da):40,384
    Last modified:August 22, 2006 - v1
    Checksum:iB14AF6A0E95883FF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DP000009 Genomic DNA. Translation: ABF99231.1.
    AP008209 Genomic DNA. Translation: BAF13401.1.
    CM000140 Genomic DNA. Translation: EEE60058.1.
    AK098878 mRNA. Translation: BAG93788.1.
    AK120304 mRNA. Translation: BAG99960.1.
    RefSeqiNP_001051487.1. NM_001058022.1.
    UniGeneiOs.74656.

    Genome annotation databases

    EnsemblPlantsiOS03T0786100-01; OS03T0786100-01; OS03G0786100.
    OS03T0786100-02; OS03T0786100-02; OS03G0786100.
    GeneIDi4334349.
    KEGGiosa:4334349.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DP000009 Genomic DNA. Translation: ABF99231.1.
    AP008209 Genomic DNA. Translation: BAF13401.1.
    CM000140 Genomic DNA. Translation: EEE60058.1.
    AK098878 mRNA. Translation: BAG93788.1.
    AK120304 mRNA. Translation: BAG99960.1.
    RefSeqiNP_001051487.1. NM_001058022.1.
    UniGeneiOs.74656.

    3D structure databases

    ProteinModelPortaliQ10CE4.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi39947.LOC_Os03g57220.1.

    Proteomic databases

    PaxDbiQ10CE4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiOS03T0786100-01; OS03T0786100-01; OS03G0786100.
    OS03T0786100-02; OS03T0786100-02; OS03G0786100.
    GeneIDi4334349.
    KEGGiosa:4334349.

    Organism-specific databases

    GrameneiQ10CE4.

    Phylogenomic databases

    eggNOGiCOG1304.
    InParanoidiQ10CE4.
    KOiK11517.
    OMAiITSAMVV.

    Enzyme and pathway databases

    UniPathwayiUPA00951; UER00912.
    BRENDAi1.1.3.15. 4460.
    ReactomeiREACT_272074. Glyoxylate metabolism.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view]
    PfamiPF01070. FMN_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species."
      The rice chromosome 3 sequencing consortium
      Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S.
      , Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.
      Genome Res. 15:1284-1291(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    3. "The rice annotation project database (RAP-DB): 2008 update."
      The rice annotation project (RAP)
      Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: cv. Nipponbare.
    4. "The genomes of Oryza sativa: a history of duplications."
      Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
      , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
      PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    5. "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
      The rice full-length cDNA consortium
      Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Nipponbare.
    6. "Oxalate accumulation and regulation is independent of glycolate oxidase in rice leaves."
      Xu H.-W., Ji X.-M., He Z.-H., Shi W.-P., Zhu G.-H., Niu J.-K., Li B.-S., Peng X.-X.
      J. Exp. Bot. 57:1899-1908(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION.
      Strain: cv. Shishoubaimao and cv. Xiangzhongxian 2.
    7. "Interaction of rice dwarf virus outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8."
      Zhou F., Wu G., Deng W., Pu Y., Wei C., Li Y.
      FEBS Lett. 581:34-40(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RICE DWARF VIRUS P8, SUBCELLULAR LOCATION.
      Strain: cv. Xiushui 11.
    8. "Inducible antisense suppression of glycolate oxidase reveals its strong regulation over photosynthesis in rice."
      Xu H.-W., Zhang J., Zeng J., Jiang L., Liu E., Peng C., He Z.-H., Peng X.-X.
      J. Exp. Bot. 60:1799-1809(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GENE FAMILY, NOMENCLATURE.
      Strain: cv. Shishoubaimao.

    Entry informationi

    Entry nameiGLO1_ORYSJ
    AccessioniPrimary (citable) accession number: Q10CE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2011
    Last sequence update: August 22, 2006
    Last modified: July 22, 2015
    This is version 69 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Oryza sativa (rice)
      Index of Oryza sativa entries and their corresponding gene designations
    3. 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.