ID   GLO3_ORYSJ              Reviewed;         367 AA.
AC   Q7FAS1; A0A0P0WEZ5; B7E4S4;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Glycolate oxidase 3;
DE            Short=GOX 3;
DE            Short=OsGLO3;
DE            EC=1.1.3.15 {ECO:0000250|UniProtKB:P05414};
DE   AltName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO3;
DE   AltName: Full=Short chain alpha-hydroxy acid oxidase GLO3;
GN   Name=GLO3; OrderedLocusNames=Os04g0623500, LOC_Os04g53210;
GN   ORFNames=OsJ_16217, OSJNBa0053K19.8;
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=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
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] (ISOFORMS 1 AND 2).
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   GENE FAMILY, AND NOMENCLATURE.
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).
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:P05414}.
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:P05414};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC         Evidence={ECO:0000250|UniProtKB:P05414};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05414};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:P05414};
CC   -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2-
CC       phosphoglycolate: step 2/3. {ECO:0000250|UniProtKB:P05414}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P05414}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P05414}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7FAS1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7FAS1-2; Sequence=VSP_040390;
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR   EMBL; AL606645; CAE03500.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF15839.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS91083.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS91084.1; -; Genomic_DNA.
DR   EMBL; CM000141; EEE61716.1; -; Genomic_DNA.
DR   EMBL; AK060221; BAG87371.1; -; mRNA.
DR   EMBL; AK068638; BAG91005.1; -; mRNA.
DR   RefSeq; XP_015635502.1; XM_015780016.1.
DR   RefSeq; XP_015635503.1; XM_015780017.1.
DR   AlphaFoldDB; Q7FAS1; -.
DR   SMR; Q7FAS1; -.
DR   STRING; 39947.Q7FAS1; -.
DR   PaxDb; 39947-Q7FAS1; -.
DR   EnsemblPlants; Os04t0623500-01; Os04t0623500-01; Os04g0623500. [Q7FAS1-2]
DR   EnsemblPlants; Os04t0623500-02; Os04t0623500-02; Os04g0623500. [Q7FAS1-1]
DR   GeneID; 4337048; -.
DR   Gramene; Os04t0623500-01; Os04t0623500-01; Os04g0623500. [Q7FAS1-2]
DR   Gramene; Os04t0623500-02; Os04t0623500-02; Os04g0623500. [Q7FAS1-1]
DR   KEGG; osa:4337048; -.
DR   eggNOG; KOG0538; Eukaryota.
DR   HOGENOM; CLU_020639_0_0_1; -.
DR   InParanoid; Q7FAS1; -.
DR   OMA; WFQLYWL; -.
DR   OrthoDB; 276514at2759; -.
DR   PlantReactome; R-OSA-1119312; Photorespiration.
DR   PlantReactome; R-OSA-1119596; Glutamate biosynthesis I.
DR   UniPathway; UPA00951; UER00912.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000007752; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
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:SF107; FMN HYDROXY ACID DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 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.
DR   Genevisible; Q7FAS1; OS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Flavoprotein; FMN; Glycolate pathway; Oxidoreductase;
KW   Peroxisome; Photorespiration; Reference proteome.
FT   CHAIN           1..367
FT                   /note="Glycolate oxidase 3"
FT                   /id="PRO_0000403413"
FT   DOMAIN          1..360
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   MOTIF           365..367
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"
FT   VAR_SEQ         306..307
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12869764"
FT                   /id="VSP_040390"
SQ   SEQUENCE   367 AA;  40533 MW;  C1F607AE6F6AD6FB CRC64;
     MELITNVSEY EQLAKQKLPK MIYDYYASGA EDQWTLKENR EAFSRILFRP RILIDVSRIN
     MATNVLGFNI SMPIMIAPSA MQKMAHPEGE LATARAASAA GTIMTLSSWS TSSVEEVNSA
     APGIRFFQLY VYKDRNIVRQ LVRRAELAGF KAIALTVDTP RLGRREADIK NRFNLPPHLV
     LKNFEALDLG KMDKTNDSGL ASYVASQVDR SLSWTDVKWL QTITSLPILV KGVMTAEDTR
     LAVESGAAGI IVSNHGARQL DYVPATISCL EEVVREAKGR LPVFLDGGVR RGTDVFKALA
     LGASGVFIGR PVLFSLAVDG EAGVRKVLQM LRDELELTMA LSGCTSLAEI TRNHVITDSD
     RIRRSRL
//