ID   GLO1_ORYSI              Reviewed;         369 AA.
AC   B8AKX6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Glycolate oxidase 1;
DE            Short=GOX 1;
DE            Short=OsGLO1;
DE            EC=1.1.3.15 {ECO:0000250|UniProtKB:Q10CE4};
DE   AltName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO1;
DE   AltName: Full=Short chain alpha-hydroxy acid oxidase GLO1;
GN   Name=GLO1; ORFNames=OsI_13800;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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).
CC   -!- FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a
CC       reduction of O2 to H2O2 (By similarity). Is a key enzyme in
CC       photorespiration in plants (By similarity). Can exert a strong
CC       regulation over photosynthesis, possibly through a feed-back inhibition
CC       on Rubisco activase. Does not seem to play a role in oxalate
CC       accumulation (By similarity). {ECO:0000250|UniProtKB:A0A3L6E0R4,
CC       ECO:0000250|UniProtKB:Q10CE4}.
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:0000250|UniProtKB:Q10CE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC         Evidence={ECO:0000250|UniProtKB:Q10CE4};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05414};
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P05414, ECO:0000250|UniProtKB:Q10CE4}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q10CE4}.
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR   EMBL; CM000128; EEC76290.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8AKX6; -.
DR   SMR; B8AKX6; -.
DR   STRING; 39946.B8AKX6; -.
DR   EnsemblPlants; BGIOSGA013686-TA; BGIOSGA013686-PA; BGIOSGA013686.
DR   Gramene; BGIOSGA013686-TA; BGIOSGA013686-PA; BGIOSGA013686.
DR   HOGENOM; CLU_020639_0_0_1; -.
DR   OMA; NEGITYI; -.
DR   UniPathway; UPA00951; UER00912.
DR   Proteomes; UP000007015; Chromosome 3.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; ISS:UniProtKB.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0098586; P:cellular response to virus; ISS:UniProtKB.
DR   GO; GO:0009854; P:oxidative photosynthetic carbon pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009853; P:photorespiration; ISS:UniProtKB.
DR   GO; GO:0010109; P:regulation of photosynthesis; ISS:UniProtKB.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   PANTHER; PTHR10578:SF115; GLYCOLATE OXIDASE 1; 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   SMART; SM01240; IMPDH; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
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_0000403410"
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
//