ID   GLO5_ORYSI              Reviewed;         369 AA.
AC   B8B7C5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Glycolate oxidase 5;
DE            Short=GOX 5;
DE            Short=OsGLO5;
DE            EC=1.1.3.15 {ECO:0000250|UniProtKB:Q9LRR9};
DE   AltName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO5;
DE   AltName: Full=Short chain alpha-hydroxy acid oxidase GLO5;
GN   Name=GLO5; ORFNames=OsI_24928;
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. Is a key enzyme in photorespiration in green
CC       plants. {ECO:0000250|UniProtKB:Q9LRR9}.
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:Q9LRR9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC         Evidence={ECO:0000250|UniProtKB:Q9LRR9};
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:Q9LRR9}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P05414}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR   EMBL; CM000132; EEC81529.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8B7C5; -.
DR   SMR; B8B7C5; -.
DR   STRING; 39946.B8B7C5; -.
DR   EnsemblPlants; BGIOSGA025165-TA; BGIOSGA025165-PA; BGIOSGA025165.
DR   Gramene; BGIOSGA025165-TA; BGIOSGA025165-PA; BGIOSGA025165.
DR   HOGENOM; CLU_020639_0_0_1; -.
DR   OMA; RIWFRPK; -.
DR   UniPathway; UPA00951; UER00912.
DR   Proteomes; UP000007015; Chromosome 7.
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:SF148; GLYCOLATE OXIDASE 5; 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   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; Oxidoreductase; Peroxisome;
KW   Photorespiration; Reference proteome.
FT   CHAIN           1..369
FT                   /note="Glycolate oxidase 5"
FT                   /id="PRO_0000403418"
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                   ECO:0000255|PROSITE-ProRule:PRU00683"
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;  40245 MW;  FE652FD1115F2681 CRC64;
     MGEITNVTEY QAIAKQKLPK MIYDYYASGA EDEWTLQENR EAFARILFRP RILIDVSKID
     MATTVLGFKI SMPIMIAPSA MQKMAHPDGE YATARAASAA GTIMTLSSWA TSSVEEVAST
     GPGIRFFQLY VYKDRRVVEQ LVRRAERAGF KAIALTVDTP RLGRREADIK NRFVLPPFLT
     LKNFEGLELG KMDQASDSGL ASYVAGQIDR TLSWKDVKWL QTITTLPILV KGVITAEDTR
     LAVENGAAGI IVSNHGARQL DYVPATISAL EEVVKAARGQ LPVFLDGGVR RGTDVFKALA
     LGAAGVFIGR PVVFSLAAAG EAGVRNVLQM LRDEFELTMA LSGCTSLADI TRNHVITEAD
     KLGVMPSRL
//