ID   GLO2_ORYSJ              Reviewed;         368 AA.
AC   Q7XPR4; B9FCL2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   02-SEP-2026, entry version 98.
DE   RecName: Full=Glycolate oxidase 2;
DE            Short=GOX 2;
DE            Short=OsGLO2;
DE            EC=1.1.3.15 {ECO:0000250|UniProtKB:P05414};
DE   AltName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO2;
DE   AltName: Full=Short chain alpha-hydroxy acid oxidase GLO2;
GN   Name=GLO2; OrderedLocusNames=Os04g0623600, LOC_Os04g53214;
GN   ORFNames=OsJ_16218, OSJNBa0053K19.9;
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=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   [4]
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   [5]
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   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE03501.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EEE61717.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL606645; CAE03501.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000141; EEE61717.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q7XPR4; -.
DR   SMR; Q7XPR4; -.
DR   FunCoup; Q7XPR4; 810.
DR   STRING; 39947.Q7XPR4; -.
DR   PaxDb; 39947-Q7XPR4; -.
DR   eggNOG; KOG0538; Eukaryota.
DR   InParanoid; Q7XPR4; -.
DR   PlantReactome; R-OSA-1119312; Photorespiration.
DR   PlantReactome; R-OSA-1119596; Glutamate biosynthesis I.
DR   UniPathway; UPA00951; UER00912.
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:0047639; F:alcohol oxidase activity; IEA:RHEA.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-ARBA.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:UniProtKB-ARBA.
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   GO; GO:0046718; P:symbiont entry into host cell; ISS:UniProtKB.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   FunFam; 3.20.20.70:FF:000204; Peroxisomal (S)-2-hydroxy-acid oxidase GLO4; 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:SF72; GLYCOLATE OXIDASE 2; 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..368
FT                   /note="Glycolate oxidase 2"
FT                   /id="PRO_0000403411"
FT   DOMAIN          1..360
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   MOTIF           366..368
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         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         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   368 AA;  40593 MW;  51A836116454D1F2 CRC64;
     MALVTNVCEY EELAKHKLPK MVYDFYAVDA EDQWTLRENS EAFSRILFQP VVLVDVSCID
     MSMSVLGYNI SMPIMIAPTA LHKLAHPEGE LATARAAAAA ETIMTLSSWS SCSIEEVNLA
     GPGVRFFQLS IYKDRNLVQQ LIQRAEKAGY KAIVLTVDAP WLGRREADVK NRFTLPQNVM
     LKIFEGLDQG KIDETNGSGL AAYVASQIDR SFSWKDIKWL QTVTSLPVLV KGIITAQDTR
     IAIEYGAAGI IMSNHGGRQL DYLPATISCL EEVVREANGR VPVFIDSGFR RGTDVFKALA
     LGASGVFIGR PVLFSLAIDG EAGVRNALRM LRDELEITMA LSGCTSVKEI TRGHVVTESD
     RIRRCSRL
//