Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9LJH5

- GLO4_ARATH

UniProt

Q9LJH5 - GLO4_ARATH

Protein

Peroxisomal (S)-2-hydroxy-acid oxidase GLO4

Gene

GLO4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Cofactori

    FMN.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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 sitei228 – 2281FMNPROSITE-ProRule annotation
    Active sitei252 – 2521Proton acceptorPROSITE-ProRule annotation
    Binding sitei255 – 2551SubstratePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi283 – 30725FMNPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. defense response to bacterium Source: TAIR
    2. hydrogen peroxide biosynthetic process Source: TAIR
    3. oxidative photosynthetic carbon pathway Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolate pathway, Photorespiration

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BioCyciARA:AT3G14130-MONOMER.
    UniPathwayiUPA00951; UER00912.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal (S)-2-hydroxy-acid oxidase GLO4 (EC:1.1.3.15)
    Alternative name(s):
    Glycolate oxidase 4
    Short name:
    AtGLO4
    Short name:
    GOX 4
    Short chain alpha-hydroxy acid oxidase GLO4
    Gene namesi
    Name:GLO4
    Ordered Locus Names:At3g14130
    ORF Names:MAG2.2
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G14130.

    Subcellular locationi

    Peroxisome By similarity

    GO - Cellular componenti

    1. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 363363Peroxisomal (S)-2-hydroxy-acid oxidase GLO4PRO_0000403407Add
    BLAST

    Proteomic databases

    PaxDbiQ9LJH5.
    PRIDEiQ9LJH5.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9LJH5.

    Interactioni

    Subunit structurei

    Homotetramer or homooctamer.By similarity

    Protein-protein interaction databases

    STRINGi3702.AT3G14130.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LJH5.
    SMRiQ9LJH5. Positions 3-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 357357FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi361 – 3633Microbody 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.
    HOGENOMiHOG000217463.
    InParanoidiQ9LJH5.
    KOiK11517.
    OMAiESCWVIV.
    PhylomeDBiQ9LJH5.

    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.

    Q9LJH5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQIVNVDEF QELAKQALPK MYYDFYNGGA EDQHTLNENV QAFRRIMFRP    50
    RVLVDVSNID MSTSMLGYPI SAPIMIAPTA MHKLAHPKGE IATAKAAAAC 100
    NTIMIVSFMS TCTIEEVASS CNAVRFLQIY VYKRRDVTAQ IVKRAEKAGF 150
    KAIVLTVDVP RLGRREADIK NKMISPQLKN FEGLVSTEVR PNEGSGVEAF 200
    ASSAFDASLS WKDIEWLRSI TKLPILVKGL LTREDALKAV EAGVDGIVVS 250
    NHGARQLDYS PATITVLEEV VHAVKGRIPV LLDGGVRRGT DVFKALALGA 300
    QAVLIGRPIV YGLAAKGEDG VKKVIDMLKN EFEITMALSG CPTIDDVTRN 350
    HVRTENERIK SML 363
    Length:363
    Mass (Da):39,878
    Last modified:October 1, 2000 - v1
    Checksum:i19A62CDD8F9E1088
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651M → I in AAM61594. 1 PublicationCurated
    Sequence conflicti107 – 1071S → P in AAM61594. 1 PublicationCurated
    Sequence conflicti273 – 2731A → V in AAM61594. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP000600 Genomic DNA. Translation: BAB02977.1.
    CP002686 Genomic DNA. Translation: AEE75475.1.
    BT002739 mRNA. Translation: AAO22568.1.
    AY085037 mRNA. Translation: AAM61594.1.
    RefSeqiNP_188029.1. NM_112269.3.
    UniGeneiAt.39288.
    At.42696.

    Genome annotation databases

    EnsemblPlantsiAT3G14130.1; AT3G14130.1; AT3G14130.
    GeneIDi820630.
    KEGGiath:AT3G14130.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP000600 Genomic DNA. Translation: BAB02977.1 .
    CP002686 Genomic DNA. Translation: AEE75475.1 .
    BT002739 mRNA. Translation: AAO22568.1 .
    AY085037 mRNA. Translation: AAM61594.1 .
    RefSeqi NP_188029.1. NM_112269.3.
    UniGenei At.39288.
    At.42696.

    3D structure databases

    ProteinModelPortali Q9LJH5.
    SMRi Q9LJH5. Positions 3-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT3G14130.1-P.

    Proteomic databases

    PaxDbi Q9LJH5.
    PRIDEi Q9LJH5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G14130.1 ; AT3G14130.1 ; AT3G14130 .
    GeneIDi 820630.
    KEGGi ath:AT3G14130.

    Organism-specific databases

    TAIRi AT3G14130.

    Phylogenomic databases

    eggNOGi COG1304.
    HOGENOMi HOG000217463.
    InParanoidi Q9LJH5.
    KOi K11517.
    OMAi ESCWVIV.
    PhylomeDBi Q9LJH5.

    Enzyme and pathway databases

    UniPathwayi UPA00951 ; UER00912 .
    BioCyci ARA:AT3G14130-MONOMER.

    Miscellaneous databases

    PROi Q9LJH5.

    Gene expression databases

    Genevestigatori Q9LJH5.

    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. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
      Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
      DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiGLO4_ARATH
    AccessioniPrimary (citable) accession number: Q9LJH5
    Secondary accession number(s): Q8LF60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2011
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 96 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3