GLO1_ARATH
ID GLO1_ARATH Reviewed; 367 AA.
AC Q9LRR9; B9DHI6; Q8VZA4; Q944K6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glycolate oxidase 1;
DE Short=AtGLO1;
DE Short=GOX1 {ECO:0000303|PubMed:25416784};
DE EC=1.1.3.15 {ECO:0000269|PubMed:25416784};
DE AltName: Full=(S)-2-hydroxy-acid oxidase GLO1;
DE AltName: Full=Short chain alpha-hydroxy acid oxidase GLO1;
GN Name=GLO1; OrderedLocusNames=At3g14420; ORFNames=MAO2.2;
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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, 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:25416784). Is a key enzyme in
CC photorespiration in green plants (Probable).
CC {ECO:0000269|PubMed:25416784, 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:25416784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC Evidence={ECO:0000305|PubMed:25416784};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05414};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for glycolate (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:25416784};
CC Note=kcat is 29.86 sec(-1) (at pH 8 and 30 degrees Celsius).
CC {ECO:0000269|PubMed:25416784};
CC -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2-
CC phosphoglycolate: step 2/3. {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=2;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LRR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LRR9-2; Sequence=VSP_040387;
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL38298.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB028617; BAB01334.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75518.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75520.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75521.1; -; Genomic_DNA.
DR EMBL; AY053412; AAK96642.1; -; mRNA.
DR EMBL; AF428396; AAL16164.1; -; mRNA.
DR EMBL; AF428328; AAL16258.1; -; mRNA.
DR EMBL; AY065122; AAL38298.1; ALT_INIT; mRNA.
DR EMBL; AY074830; AAL69528.1; -; mRNA.
DR EMBL; AY081566; AAM10128.1; -; mRNA.
DR EMBL; AK317539; BAH20203.1; -; mRNA.
DR RefSeq; NP_001030694.1; NM_001035617.1. [Q9LRR9-2]
DR RefSeq; NP_188060.1; NM_112302.4. [Q9LRR9-1]
DR RefSeq; NP_850584.1; NM_180253.2. [Q9LRR9-1]
DR AlphaFoldDB; Q9LRR9; -.
DR SMR; Q9LRR9; -.
DR BioGRID; 5999; 5.
DR IntAct; Q9LRR9; 3.
DR MINT; Q9LRR9; -.
DR STRING; 3702.AT3G14420.1; -.
DR iPTMnet; Q9LRR9; -.
DR PaxDb; Q9LRR9; -.
DR PRIDE; Q9LRR9; -.
DR EnsemblPlants; AT3G14420.1; AT3G14420.1; AT3G14420. [Q9LRR9-1]
DR EnsemblPlants; AT3G14420.2; AT3G14420.2; AT3G14420. [Q9LRR9-1]
DR EnsemblPlants; AT3G14420.4; AT3G14420.4; AT3G14420. [Q9LRR9-2]
DR GeneID; 820665; -.
DR Gramene; AT3G14420.1; AT3G14420.1; AT3G14420. [Q9LRR9-1]
DR Gramene; AT3G14420.2; AT3G14420.2; AT3G14420. [Q9LRR9-1]
DR Gramene; AT3G14420.4; AT3G14420.4; AT3G14420. [Q9LRR9-2]
DR KEGG; ath:AT3G14420; -.
DR Araport; AT3G14420; -.
DR TAIR; locus:2091642; AT3G14420.
DR eggNOG; KOG0538; Eukaryota.
DR InParanoid; Q9LRR9; -.
DR PhylomeDB; Q9LRR9; -.
DR BioCyc; ARA:AT3G14420-MON; -.
DR BioCyc; MetaCyc:AT3G14420-MON; -.
DR BRENDA; 1.1.3.15; 399.
DR UniPathway; UPA00951; UER00912.
DR PRO; PR:Q9LRR9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRR9; baseline and differential.
DR Genevisible; Q9LRR9; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:TAIR.
DR GO; GO:0009854; P:oxidative photosynthetic carbon pathway; IEA:UniProtKB-UniPathway.
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 1"
FT /id="PRO_0000206324"
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"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040387"
FT CONFLICT 55
FT /note="V -> A (in Ref. 3; AAL16258)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="P -> L (in Ref. 3; AAL38298/AAM10128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40341 MW; B107AD7AC983A04C CRC64;
MEITNVTEYD AIAKQKLPKM VYDYYASGAE DQWTLQENRN AFARILFRPR ILIDVSKIDM
TTTVLGFKIS MPIMVAPTAM QKMAHPDGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG
PGIRFFQLYV YKNRNVVEQL VRRAERAGFK AIALTVDTPR LGRRESDIKN RFTLPPNLTL
KNFEGLDLGK MDEANDSGLA SYVAGQIDRT LSWKDVQWLQ TITKLPILVK GVLTGEDARI
AIQAGAAGII VSNHGARQLD YVPATISALE EVVKATQGRI PVFLDGGVRR GTDVFKALAL
GASGIFIGRP VVFSLAAEGE AGVRKVLQML RDEFELTMAL SGCRSLKEIS RNHITTEWDT
PRPSARL
