HAOX2_ARATH
ID HAOX2_ARATH Reviewed; 363 AA.
AC Q24JJ8; Q8L8P3; Q9LJH3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Peroxisomal (S)-2-hydroxyacid oxidase GLO3;
DE EC=1.1.3.15 {ECO:0000269|PubMed:24408912};
DE AltName: Full=Glycolate oxidase 3;
DE Short=AtGLO3;
DE Short=GOX 3;
DE AltName: Full=Short chain alpha-hydroxy acid oxidase GLO3;
DE AltName: Full=lHAOX2 {ECO:0000303|PubMed:24408912};
GN Name=GLO3; OrderedLocusNames=At3g14150; ORFNames=MAG2.11;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19329564; DOI=10.1104/pp.109.137703;
RA Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D.,
RA Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.;
RT "In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with
RT in vivo subcellular targeting verification indicates novel metabolic and
RT regulatory functions of peroxisomes.";
RL Plant Physiol. 150:125-143(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=24408912; DOI=10.1093/molbev/msu041;
RA Esser C., Kuhn A., Groth G., Lercher M.J., Maurino V.G.;
RT "Plant and animal glycolate oxidases have a common eukaryotic ancestor and
RT convergently duplicated to evolve long-chain 2-hydroxy acid oxidases.";
RL Mol. Biol. Evol. 31:1089-1101(2014).
CC -!- FUNCTION: Oxidase that catalyzes the oxidation of a broad range of 2-
CC hydroxyacids to the corresponding 2-oxoacids, with a reduction of O2 to
CC H2O2. Displays the highest activity with leucic acid (2-hydroxy-4-
CC methylpentanoate) and has intermediate activity with 2-hydroxyhexanoate
CC and 2-hydroxyoctanote. Shows lower activity with 2-hydroxydodecanoate,
CC valic acid, and isoleucic acid and extremely low activity with
CC glycolate and L-lactate. Cannot use 2-hydroxyhexadecanoate or D-lactate
CC as substrates. May be involved in the conversion or degradation of 2-
CC hydroxyacids produced during the metabolism of fatty acids or amino
CC acids. {ECO:0000269|PubMed:24408912}.
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:24408912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790;
CC Evidence={ECO:0000305|PubMed:24408912};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-4-methylpentanoate + O2 = 4-methyl-2-oxopentanoate +
CC H2O2; Xref=Rhea:RHEA:69380, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:133577;
CC Evidence={ECO:0000269|PubMed:24408912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69381;
CC Evidence={ECO:0000305|PubMed:24408912};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyhexanoate + O2 = 2-oxohexanoate + H2O2;
CC Xref=Rhea:RHEA:69372, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:35177, ChEBI:CHEBI:133738;
CC Evidence={ECO:0000269|PubMed:24408912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69373;
CC Evidence={ECO:0000305|PubMed:24408912};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctanoate + O2 = 2-oxooctanoate + H2O2;
CC Xref=Rhea:RHEA:67940, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:133514, ChEBI:CHEBI:176689;
CC Evidence={ECO:0000269|PubMed:24408912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67941;
CC Evidence={ECO:0000305|PubMed:24408912};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05414};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P05414}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305|PubMed:19329564}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02979.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000600; BAB02979.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75477.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75478.1; -; Genomic_DNA.
DR EMBL; BT024891; ABD85162.1; -; mRNA.
DR EMBL; AY088888; AAM67194.1; -; mRNA.
DR RefSeq; NP_001078152.1; NM_001084683.2.
DR RefSeq; NP_188031.1; NM_112271.4.
DR AlphaFoldDB; Q24JJ8; -.
DR SMR; Q24JJ8; -.
DR STRING; 3702.AT3G14150.1; -.
DR PaxDb; Q24JJ8; -.
DR PRIDE; Q24JJ8; -.
DR ProteomicsDB; 248577; -.
DR EnsemblPlants; AT3G14150.1; AT3G14150.1; AT3G14150.
DR EnsemblPlants; AT3G14150.2; AT3G14150.2; AT3G14150.
DR GeneID; 820632; -.
DR Gramene; AT3G14150.1; AT3G14150.1; AT3G14150.
DR Gramene; AT3G14150.2; AT3G14150.2; AT3G14150.
DR KEGG; ath:AT3G14150; -.
DR Araport; AT3G14150; -.
DR TAIR; locus:2087517; AT3G14150.
DR eggNOG; KOG0538; Eukaryota.
DR HOGENOM; CLU_020639_1_0_1; -.
DR InParanoid; Q24JJ8; -.
DR OMA; WIAVHSK; -.
DR OrthoDB; 879633at2759; -.
DR PhylomeDB; Q24JJ8; -.
DR BioCyc; ARA:AT3G14150-MON; -.
DR BRENDA; 1.1.3.15; 399.
DR PRO; PR:Q24JJ8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q24JJ8; baseline and differential.
DR Genevisible; Q24JJ8; AT.
DR GO; GO:0005777; C:peroxisome; IDA: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:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:TAIR.
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 Flavoprotein; FMN; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..363
FT /note="Peroxisomal (S)-2-hydroxyacid oxidase GLO3"
FT /id="PRO_0000403406"
FT DOMAIN 1..357
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT MOTIF 361..363
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05414"
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="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 165
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 228
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 250
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 255
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 283..287
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 306..307
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT CONFLICT 87
FT /note="P -> L (in Ref. 4; AAM67194)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="I -> M (in Ref. 4; AAM67194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40130 MW; 8AA94B1A354BA60C CRC64;
MDQIVNVDEF QELAKQALPK MYYDFYNGGA EDQHTLNENV QAFRRIMFRP RVLVDVSKID
MSTKILGYPI SAPIMIAPTG NHKLAHPEGE TATAKAAAAC NTIMIVSYMS SCTFEEIASS
CNAVRFLQIY VYKRRDITAQ VVKRAEKAGF KAIVLTVDVP RLGRREADIK NKMISPQLKN
FEGLFSTEVR PSKGSGVQAF ASRAFDASFS WKDIEWLRSI TELPILVKGI LTREDALKAV
EAGVDGIIVS NHGGRQLDYS PATITVLEEV VQVVRGRIPV LLDGGVRRGT DVFKALALGA
QAVLIGRPII YGLAAKGEDG VKKVIDMLKN EFEITMALSG CPTIDDITRN HVRTENERLH
SML
