GLO2_ARATH
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 03-AUG-2022, entry version 153.
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; 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=0.30 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.AT3G14415.2; -.
DR iPTMnet; Q9LRS0; -.
DR PaxDb; Q9LRS0; -.
DR PRIDE; Q9LRS0; -.
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 eggNOG; KOG0538; Eukaryota.
DR HOGENOM; CLU_020639_0_0_1; -.
DR InParanoid; Q9LRS0; -.
DR PhylomeDB; Q9LRS0; -.
DR BioCyc; ARA:AT3G14415-MON; -.
DR UniPathway; UPA00951; UER00912.
DR PRO; PR:Q9LRS0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRS0; baseline and differential.
DR Genevisible; Q9LRS0; AT.
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; -; 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 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
