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B8B7C5

- GLO5_ORYSI

UniProt

B8B7C5 - GLO5_ORYSI

Protein

Peroxisomal (S)-2-hydroxy-acid oxidase GLO5

Gene

GLO5

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (03 Mar 2009)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    FMN.PROSITE-ProRule annotations

    Pathwayi

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. FMN binding Source: InterPro
    2. glycolate oxidase activity Source: UniProtKB
    3. long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
    4. medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
    5. very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. modulation by virus of host morphology or physiology Source: UniProtKB
    2. oxidative photosynthetic carbon pathway Source: UniProtKB-UniPathway
    3. photorespiration Source: UniProtKB
    4. regulation of photosynthesis Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolate pathway, Host-virus interaction, Photorespiration

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    UniPathwayiUPA00951; UER00912.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal (S)-2-hydroxy-acid oxidase GLO5 (EC:1.1.3.15)
    Alternative name(s):
    Glycolate oxidase 5
    Short name:
    GOX 5
    Short name:
    OsGLO5
    Short chain alpha-hydroxy acid oxidase GLO5
    Gene namesi
    Name:GLO5
    ORF Names:OsI_24928
    OrganismiOryza sativa subsp. indica (Rice)
    Taxonomic identifieri39946 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

    Organism-specific databases

    GrameneiB8B7C5.

    Subcellular locationi

    Peroxisome By similarity

    GO - Cellular componenti

    1. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 369369Peroxisomal (S)-2-hydroxy-acid oxidase GLO5PRO_0000403418Add
    BLAST

    Proteomic databases

    PRIDEiB8B7C5.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi39947.LOC_Os07g05820.2.

    Structurei

    3D structure databases

    ProteinModelPortaliB8B7C5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 360360FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationsAdd
    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 annotations
    Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotations

    Phylogenomic databases

    eggNOGiCOG1304.
    HOGENOMiHOG000217463.

    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...

    Sequencei

    Sequence statusi: Complete.

    B8B7C5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGEITNVTEY QAIAKQKLPK MIYDYYASGA EDEWTLQENR EAFARILFRP    50
    RILIDVSKID MATTVLGFKI SMPIMIAPSA MQKMAHPDGE YATARAASAA 100
    GTIMTLSSWA TSSVEEVAST GPGIRFFQLY VYKDRRVVEQ LVRRAERAGF 150
    KAIALTVDTP RLGRREADIK NRFVLPPFLT LKNFEGLELG KMDQASDSGL 200
    ASYVAGQIDR TLSWKDVKWL QTITTLPILV KGVITAEDTR LAVENGAAGI 250
    IVSNHGARQL DYVPATISAL EEVVKAARGQ LPVFLDGGVR RGTDVFKALA 300
    LGAAGVFIGR PVVFSLAAAG EAGVRNVLQM LRDEFELTMA LSGCTSLADI 350
    TRNHVITEAD KLGVMPSRL 369
    Length:369
    Mass (Da):40,245
    Last modified:March 3, 2009 - v1
    Checksum:iFE652FD1115F2681
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000132 Genomic DNA. Translation: EEC81529.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000132 Genomic DNA. Translation: EEC81529.1 .

    3D structure databases

    ProteinModelPortali B8B7C5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 39947.LOC_Os07g05820.2.

    Proteomic databases

    PRIDEi B8B7C5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei B8B7C5.

    Phylogenomic databases

    eggNOGi COG1304.
    HOGENOMi HOG000217463.

    Enzyme and pathway databases

    UniPathwayi UPA00951 ; UER00912 .

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view ]
    Pfami PF01070. FMN_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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. 93-11.

    Entry informationi

    Entry nameiGLO5_ORYSI
    AccessioniPrimary (citable) accession number: B8B7C5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2011
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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