ID GLO5_ORYSJ Reviewed; 369 AA. AC Q6YT73; A0A0P0X2P6; B9FVJ4; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 12-OCT-2022, entry version 124. DE RecName: Full=Glycolate oxidase 5; DE Short=GOX 3; 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; OrderedLocusNames=Os07g0152900, LOC_Os07g05820; GN ORFNames=B1364A02.33-1, OsJ_23125, OSJNBb0050B07.1-1; 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=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 [2] 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 [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 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 [6] 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: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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP005632; BAD31578.1; -; Genomic_DNA. DR EMBL; AP006163; BAC84719.1; -; Genomic_DNA. DR EMBL; AP008213; BAF20823.1; -; Genomic_DNA. DR EMBL; AP014963; BAT00100.1; -; Genomic_DNA. DR EMBL; CM000144; EEE66581.1; -; Genomic_DNA. DR EMBL; AK062189; BAG88242.1; -; mRNA. DR EMBL; AK103933; BAG96328.1; -; mRNA. DR RefSeq; XP_015646859.1; XM_015791373.1. DR AlphaFoldDB; Q6YT73; -. DR SMR; Q6YT73; -. DR STRING; 4530.OS07T0152900-01; -. DR PaxDb; Q6YT73; -. DR EnsemblPlants; Os07t0152900-01; Os07t0152900-01; Os07g0152900. DR EnsemblPlants; Os07t0152900-03; Os07t0152900-03; Os07g0152900. DR EnsemblPlants; Os07t0152900-04; Os07t0152900-04; Os07g0152900. DR GeneID; 4342420; -. DR Gramene; Os07t0152900-01; Os07t0152900-01; Os07g0152900. DR Gramene; Os07t0152900-03; Os07t0152900-03; Os07g0152900. DR Gramene; Os07t0152900-04; Os07t0152900-04; Os07g0152900. DR KEGG; osa:4342420; -. DR eggNOG; KOG0538; Eukaryota. DR HOGENOM; CLU_020639_0_0_1; -. DR InParanoid; Q6YT73; -. DR OMA; FTRLMQT; -. DR OrthoDB; 879633at2759; -. DR PlantReactome; R-OSA-1119312; Photorespiration. DR PlantReactome; R-OSA-1119596; Glutamate biosynthesis I. DR UniPathway; UPA00951; UER00912. DR Proteomes; UP000000763; Chromosome 7. DR Proteomes; UP000007752; Chromosome 7. DR Proteomes; UP000059680; Chromosome 7. DR ExpressionAtlas; Q6YT73; baseline and differential. DR Genevisible; Q6YT73; OS. 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; -; 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 2: Evidence at transcript level; KW Flavoprotein; FMN; Glycolate pathway; Oxidoreductase; Peroxisome; KW Photorespiration; Reference proteome. FT CHAIN 1..369 FT /note="Glycolate oxidase 5" FT /id="PRO_0000403417" 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" FT CONFLICT 265 FT /note="A -> S (in Ref. 4; EEE66581)" FT /evidence="ECO:0000305" 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 //