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 07-OCT-2020, entry version 118. DE RecName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO5; DE EC=1.1.3.15; DE AltName: Full=Glycolate oxidase 5; DE Short=GOX 5; DE Short=OsGLO5; 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: Photorespiratory enzyme that can exert a strong regulation CC over photosynthesis, possibly through a feed-back inhibition on Rubisco CC activase. Not required for oxalate accumulation (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2; CC Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00683}; CC -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2- CC phosphoglycolate: step 2/3. CC -!- SUBUNIT: Homotetramer or homooctamer. Interacts with rice dwarf virus CC (RDV) P8. This interaction promotes viral P8 relocation to virus CC factories peripheral to peroxisomes (By similarity). {ECO:0000250}. 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 SMR; Q6YT73; -. DR STRING; 4530.OS07T0152900-01; -. DR PaxDb; Q6YT73; -. DR PRIDE; 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 KO; K11517; -. DR OMA; RIWFRPQ; -. 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:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0008891; F:glycolate oxidase activity; ISS:UniProtKB. DR GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0019048; P:modulation by virus of host process; 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; Host-virus interaction; KW Oxidoreductase; Peroxisome; Photorespiration; Reference proteome. FT CHAIN 1..369 FT /note="Peroxisomal (S)-2-hydroxy-acid oxidase GLO5" FT /id="PRO_0000403417" FT DOMAIN 1..360 FT /note="FMN hydroxy acid dehydrogenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT NP_BIND 286..310 FT /note="FMN" 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:0000255|PROSITE-ProRule:PRU00683" FT BINDING 25 FT /note="Substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT BINDING 107 FT /note="FMN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT BINDING 128 FT /note="FMN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT BINDING 130 FT /note="Substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT BINDING 156 FT /note="FMN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT BINDING 165 FT /note="Substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT BINDING 231 FT /note="FMN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT BINDING 258 FT /note="Substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" 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 //