GLO1_ORYSJ
ID GLO1_ORYSJ Reviewed; 369 AA.
AC Q10CE4; A0A0P0W4I1;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glycolate oxidase 1;
DE Short=GOX 1;
DE Short=OsGLO1;
DE EC=1.1.3.15 {ECO:0000269|PubMed:16595582};
DE AltName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO1;
DE AltName: Full=Short chain alpha-hydroxy acid oxidase GLO1;
GN Name=GLO1; Synonyms=GOX; OrderedLocusNames=Os03g0786100, LOC_Os03g57220;
GN ORFNames=OsJ_12861;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Shishoubaimao, and cv. Xiangzhongxian 2;
RX PubMed=16595582; DOI=10.1093/jxb/erj131;
RA Xu H.-W., Ji X.-M., He Z.-H., Shi W.-P., Zhu G.-H., Niu J.-K., Li B.-S.,
RA Peng X.-X.;
RT "Oxalate accumulation and regulation is independent of glycolate oxidase in
RT rice leaves.";
RL J. Exp. Bot. 57:1899-1908(2006).
RN [8]
RP INTERACTION WITH RICE DWARF VIRUS P8, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Xiushui 11;
RX PubMed=17174956; DOI=10.1016/j.febslet.2006.11.073;
RA Zhou F., Wu G., Deng W., Pu Y., Wei C., Li Y.;
RT "Interaction of rice dwarf virus outer capsid P8 protein with rice
RT glycolate oxidase mediates relocalization of P8.";
RL FEBS Lett. 581:34-40(2007).
RN [9]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Shishoubaimao;
RX PubMed=19264754; DOI=10.1093/jxb/erp056;
RA Xu H.-W., Zhang J., Zeng J., Jiang L., Liu E., Peng C., He Z.-H.,
RA Peng X.-X.;
RT "Inducible antisense suppression of glycolate oxidase reveals its strong
RT regulation over photosynthesis in rice.";
RL J. Exp. Bot. 60:1799-1809(2009).
RN [10]
RP INTERACTION WITH CATB AND CATC.
RC STRAIN=cv. Zhonghua 11;
RX PubMed=26900141; DOI=10.1016/j.molp.2016.02.002;
RA Zhang Z., Xu Y., Xie Z., Li X., He Z.-H., Peng X.-X.;
RT "Association-dissociation of glycolate oxidase with catalase in rice: a
RT potential switch to modulate intracellular H2O2 levels.";
RL Mol. Plant 9:737-748(2016).
CC -!- FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a
CC reduction of O2 to H2O2 (PubMed:16595582). Is a key enzyme in
CC photorespiration in plants (By similarity). To a lesser extent, is also
CC able to oxidize glyoxylate to oxalate in vitro (PubMed:16595582). Can
CC exert a strong regulation over photosynthesis, possibly through a feed-
CC back inhibition on Rubisco activase (PubMed:19264754). Does not seem to
CC play a role in oxalate accumulation (PubMed:16595582).
CC {ECO:0000250|UniProtKB:A0A3L6E0R4, ECO:0000269|PubMed:16595582,
CC ECO:0000269|PubMed:19264754}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycolate + O2 = glyoxylate + H2O2; Xref=Rhea:RHEA:25311,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:36655; EC=1.1.3.15;
CC Evidence={ECO:0000269|PubMed:16595582};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC Evidence={ECO:0000305|PubMed:16595582};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05414};
CC -!- ACTIVITY REGULATION: Competitively inhibited by oxalate.
CC {ECO:0000269|PubMed:16595582}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for glycolate (at pH 8.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16595582};
CC KM=4 mM for glyoxylate (at pH 8.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16595582};
CC -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2-
CC phosphoglycolate: step 2/3. {ECO:0000250|UniProtKB:A0A3L6E0R4}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with rice dwarf virus
CC (RDV) P8. This interaction promotes viral P8 relocation to virus
CC factories peripheral to peroxisomes. Binds to CATB and CATC; these
CC interactions are disturbed by alpha-hydroxy-2-pyridinemethanesulfonic
CC acid (HPMS) and salicylic acid (SA) (PubMed:26900141).
CC {ECO:0000250|UniProtKB:P05414, ECO:0000269|PubMed:17174956,
CC ECO:0000269|PubMed:26900141}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17174956}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in leaves (at protein
CC level). {ECO:0000269|PubMed:16595582}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR EMBL; DP000009; ABF99231.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13401.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86730.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE60058.1; -; Genomic_DNA.
DR EMBL; AK098878; BAG93788.1; -; mRNA.
DR EMBL; AK120304; BAG99960.1; -; mRNA.
DR AlphaFoldDB; Q10CE4; -.
DR SMR; Q10CE4; -.
DR STRING; 4530.OS03T0786100-01; -.
DR PaxDb; Q10CE4; -.
DR PRIDE; Q10CE4; -.
DR EnsemblPlants; Os03t0786100-01; Os03t0786100-01; Os03g0786100.
DR EnsemblPlants; Os03t0786100-02; Os03t0786100-02; Os03g0786100.
DR Gramene; Os03t0786100-01; Os03t0786100-01; Os03g0786100.
DR Gramene; Os03t0786100-02; Os03t0786100-02; Os03g0786100.
DR eggNOG; KOG0538; Eukaryota.
DR HOGENOM; CLU_020639_0_0_1; -.
DR InParanoid; Q10CE4; -.
DR OMA; WSYVAGG; -.
DR BRENDA; 1.1.3.15; 4460.
DR PlantReactome; R-OSA-1119312; Photorespiration.
DR PlantReactome; R-OSA-1119596; Glutamate biosynthesis I.
DR SABIO-RK; Q10CE4; -.
DR UniPathway; UPA00951; UER00912.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10CE4; OS.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0098586; P:cellular response to virus; IPI:UniProtKB.
DR GO; GO:0009854; P:oxidative photosynthetic carbon pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0009853; P:photorespiration; IMP:UniProtKB.
DR GO; GO:0010109; P:regulation of photosynthesis; IMP:UniProtKB.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Glycolate pathway; Host-virus interaction;
KW Oxidoreductase; Peroxisome; Photorespiration; Reference proteome.
FT CHAIN 1..369
FT /note="Glycolate oxidase 1"
FT /id="PRO_0000403409"
FT DOMAIN 1..360
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT MOTIF 367..369
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 25
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT BINDING 78..80
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 128..130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 130
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT BINDING 156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 165
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT BINDING 231
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 253
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 255
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT BINDING 258
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT BINDING 286..290
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 309..310
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT SITE 109
FT /note="Involved in determining the substrate specificity of
FT glycolate oxidase"
FT /evidence="ECO:0000250|UniProtKB:P05414"
SQ SEQUENCE 369 AA; 40384 MW; B14AF6A0E95883FF CRC64;
MGEITNVMEY QAIAKQKLPK MIYDYYASGA EDEWTLKENR EAFSRILFRP RILIDVSKID
MSATVLGFKI SMPIMIAPSA MQKMAHPDGE YATARAASAA GTIMTLSSWA TSSVEEVAST
GPGIRFFQLY VYKDRNVVEQ LVRRAERAGF KAIALTVDTP RLGRREADIK NRFVLPPYLT
LKNFEGLDLA EMDKSNDSGL ASYVAGQIDR TLSWKDVKWL QSITSLPILV KGVITAEDAR
LAVHSGAAGI IVSNHGARQL DYVPATISAL EEVVTAAAGR IPVYLDGGVR RGTDVFKALA
LGAAGVFIGR PVVFALAAEG EAGVRNVLRM MREEFELTMA LSGCTSLADI TRAHIYTDAD
RLARPFPRL
