ID   GLO2_ARATH              Reviewed;         367 AA.
AC   Q9LRS0; Q56XF8;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Glycolate oxidase 2;
DE            Short=AtGLO2;
DE            Short=GOX2 {ECO:0000303|PubMed:25416784};
DE            EC=1.1.3.15 {ECO:0000269|PubMed:25416784};
DE   AltName: Full=(S)-2-hydroxy-acid oxidase GLO2;
DE   AltName: Full=Short chain alpha-hydroxy acid oxidase GLO2;
GN   Name=GLO2; Synonyms=GOX1; OrderedLocusNames=At3g14415;
GN   ORFNames=MLN21.20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA   Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA   Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT   "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT   peptides, metabolic pathways, and defense mechanisms.";
RL   Plant Cell 19:3170-3193(2007).
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).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, AND PATHWAY.
RX   PubMed=21828292; DOI=10.1105/tpc.111.088070;
RA   Hackenberg C., Kern R., Huge J., Stal L.J., Tsuji Y., Kopka J.,
RA   Shiraiwa Y., Bauwe H., Hagemann M.;
RT   "Cyanobacterial lactate oxidases serve as essential partners in N2 fixation
RT   and evolved into photorespiratory glycolate oxidases in plants.";
RL   Plant Cell 23:2978-2990(2011).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION
RP   MECHANISM, ACTIVE SITE, AND PATHWAY.
RX   PubMed=25416784; DOI=10.1074/jbc.m114.618629;
RA   Dellero Y., Mauve C., Boex-Fontvieille E., Flesch V., Jossier M.,
RA   Tcherkez G., Hodges M.;
RT   "Experimental evidence for a hydride transfer mechanism in plant glycolate
RT   oxidase catalysis.";
RL   J. Biol. Chem. 290:1689-1698(2015).
CC   -!- FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a
CC       reduction of O2 to H2O2 (PubMed:21828292, PubMed:25416784). Is a key
CC       enzyme in photorespiration in green plants (Probable). Glycolate is the
CC       preferred substrate, but to a lesser extent, this oxidase is also able
CC       to use hydroxypyruvate, L-lactate and glycerate as substrates in vitro
CC       (PubMed:21828292). {ECO:0000269|PubMed:21828292,
CC       ECO:0000269|PubMed:25416784, ECO:0000305|PubMed:21828292,
CC       ECO:0000305|PubMed:25416784}.
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:0000269|PubMed:21828292, ECO:0000269|PubMed:25416784};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC         Evidence={ECO:0000305|PubMed:21828292, ECO:0000305|PubMed:25416784};
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         Evidence={ECO:0000269|PubMed:21828292, ECO:0000269|PubMed:25416784};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790;
CC         Evidence={ECO:0000305|PubMed:21828292, ECO:0000305|PubMed:25416784};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + O2 = H2O2 + pyruvate; Xref=Rhea:RHEA:55868,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16651; Evidence={ECO:0000269|PubMed:21828292};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55869;
CC         Evidence={ECO:0000305|PubMed:21828292};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05414};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.356 mM for (S)-lactate {ECO:0000269|PubMed:21828292};
CC         KM=1.906 mM for glycolate {ECO:0000269|PubMed:21828292};
CC         KM=0.3 mM for glycolate (at pH 8 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:25416784};
CC         Vmax=0.742 umol/min/mg enzyme with (S)-lactate as substrate
CC         {ECO:0000269|PubMed:21828292};
CC         Vmax=35.64 umol/min/mg enzyme with glycolate as substrate
CC         {ECO:0000269|PubMed:21828292};
CC         Note=kcat is 30.10 sec(-1) with glycolate as substrate (at pH 8 and
CC         30 degrees Celsius). {ECO:0000269|PubMed:25416784};
CC   -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2-
CC       phosphoglycolate: step 2/3. {ECO:0000305|PubMed:21828292,
CC       ECO:0000305|PubMed:25416784}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P05414}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9LRS0-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR   EMBL; AB028617; BAB01333.1; -; Genomic_DNA.
DR   EMBL; AB022220; BAB01333.1; JOINED; Genomic_DNA.
DR   EMBL; CP002686; AEE75515.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75517.1; -; Genomic_DNA.
DR   EMBL; AY058095; AAL24203.1; -; mRNA.
DR   EMBL; AY136402; AAM97068.1; -; mRNA.
DR   EMBL; BT002129; AAN72140.1; -; mRNA.
DR   EMBL; AK221716; BAD95441.1; -; mRNA.
DR   RefSeq; NP_001189892.1; NM_001202963.1. [Q9LRS0-1]
DR   RefSeq; NP_188059.1; NM_112301.3. [Q9LRS0-1]
DR   AlphaFoldDB; Q9LRS0; -.
DR   SMR; Q9LRS0; -.
DR   BioGRID; 5998; 5.
DR   IntAct; Q9LRS0; 1.
DR   STRING; 3702.Q9LRS0; -.
DR   iPTMnet; Q9LRS0; -.
DR   PaxDb; 3702-AT3G14415-2; -.
DR   ProteomicsDB; 230398; -. [Q9LRS0-1]
DR   EnsemblPlants; AT3G14415.1; AT3G14415.1; AT3G14415. [Q9LRS0-1]
DR   EnsemblPlants; AT3G14415.3; AT3G14415.3; AT3G14415. [Q9LRS0-1]
DR   GeneID; 820664; -.
DR   Gramene; AT3G14415.1; AT3G14415.1; AT3G14415. [Q9LRS0-1]
DR   Gramene; AT3G14415.3; AT3G14415.3; AT3G14415. [Q9LRS0-1]
DR   KEGG; ath:AT3G14415; -.
DR   Araport; AT3G14415; -.
DR   TAIR; AT3G14415; GOX2.
DR   eggNOG; KOG0538; Eukaryota.
DR   HOGENOM; CLU_020639_0_0_1; -.
DR   InParanoid; Q9LRS0; -.
DR   PhylomeDB; Q9LRS0; -.
DR   BioCyc; ARA:AT3G14415-MONOMER; -.
DR   UniPathway; UPA00951; UER00912.
DR   PRO; PR:Q9LRS0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LRS0; baseline and differential.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0009854; P:oxidative photosynthetic carbon pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051707; P:response to other organism; IEA:UniProt.
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:SF110; 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.
DR   Genevisible; Q9LRS0; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Flavoprotein; FMN; Glycolate pathway;
KW   Oxidoreductase; Peroxisome; Photorespiration; Reference proteome.
FT   CHAIN           1..367
FT                   /note="Glycolate oxidase 2"
FT                   /id="PRO_0000206323"
FT   DOMAIN          1..359
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   ACT_SITE        254
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683,
FT                   ECO:0000305|PubMed:25416784"
FT   BINDING         24
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT   BINDING         77..79
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         106
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         127..129
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         129
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT   BINDING         155
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         164
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT   BINDING         230
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         252
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         254
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT   BINDING         257
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT   BINDING         285..289
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         308..309
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   SITE            108
FT                   /note="Involved in determining the substrate specificity of
FT                   glycolate oxidase"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O49506"
SQ   SEQUENCE   367 AA;  40307 MW;  C0B0F9B083F1B6E6 CRC64;
     MEITNVTEYD AIAKAKLPKM VYDYYASGAE DQWTLQENRN AFARILFRPR ILIDVNKIDM
     ATTVLGFKIS MPIMVAPTAF QKMAHPDGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG
     PGIRFFQLYV YKNRKVVEQL VRRAEKAGFK AIALTVDTPR LGRRESDIKN RFTLPPNLTL
     KNFEGLDLGK MDEANDSGLA SYVAGQIDRT LSWKDIQWLQ TITNMPILVK GVLTGEDARI
     AIQAGAAGII VSNHGARQLD YVPATISALE EVVKATQGRV PVFLDGGVRR GTDVFKALAL
     GASGIFIGRP VVFALAAEGE AGVKKVLQML RDEFELTMAL SGCRSLSEIT RNHIVTEWDT
     PRHLPRL
//