HAOX1_ARATH
ID HAOX1_ARATH Reviewed; 363 AA.
AC Q9LJH5; Q8LF60;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Peroxisomal (S)-2-hydroxyacid oxidase GLO4;
DE EC=1.1.3.15 {ECO:0000269|PubMed:24408912};
DE AltName: Full=Glycolate oxidase 4;
DE Short=AtGLO4;
DE Short=GOX 4;
DE AltName: Full=lHAOX1 {ECO:0000303|PubMed:24408912};
GN Name=GLO4; OrderedLocusNames=At3g14130; ORFNames=MAG2.2;
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=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;
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].
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 FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
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 the long-chain fatty acid 2-
CC hydroxydodecanoate and has intermediate activity with 2-
CC hydroxyhexanoate, 2-hydroxyoctanote, and the short-chain hydroxyacid
CC (S)-lactate (L-lactate). With much lower activity, it can also use
CC glycolate, leucic acid, valic acid, and isoleucic acid as substrates in
CC vitro. Cannot use 2-hydroxyhexadecanoate or D-lactate as substrates.
CC May be involved in a general medium- and long-chain fatty acid
CC catabolic pathway such as alpha-oxidation.
CC {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-hydroxydodecanoate + O2 = 2-oxododecanoate + H2O2;
CC Xref=Rhea:RHEA:69376, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:141772, ChEBI:CHEBI:142579;
CC Evidence={ECO:0000269|PubMed:24408912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69377;
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 -!- 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:24408912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55869;
CC Evidence={ECO:0000305|PubMed:24408912};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05414};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:24408912}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P05414}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR EMBL; AP000600; BAB02977.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75475.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65219.1; -; Genomic_DNA.
DR EMBL; BT002739; AAO22568.1; -; mRNA.
DR EMBL; AY085037; AAM61594.1; -; mRNA.
DR RefSeq; NP_001327205.1; NM_001338103.1.
DR RefSeq; NP_188029.1; NM_112269.3.
DR AlphaFoldDB; Q9LJH5; -.
DR SMR; Q9LJH5; -.
DR STRING; 3702.AT3G14130.1; -.
DR PaxDb; Q9LJH5; -.
DR PRIDE; Q9LJH5; -.
DR EnsemblPlants; AT3G14130.1; AT3G14130.1; AT3G14130.
DR EnsemblPlants; AT3G14130.3; AT3G14130.3; AT3G14130.
DR GeneID; 820630; -.
DR Gramene; AT3G14130.1; AT3G14130.1; AT3G14130.
DR Gramene; AT3G14130.3; AT3G14130.3; AT3G14130.
DR KEGG; ath:AT3G14130; -.
DR Araport; AT3G14130; -.
DR TAIR; locus:2087487; AT3G14130.
DR eggNOG; KOG0538; Eukaryota.
DR HOGENOM; CLU_020639_6_1_1; -.
DR InParanoid; Q9LJH5; -.
DR OMA; FQYEIYL; -.
DR OrthoDB; 879633at2759; -.
DR PhylomeDB; Q9LJH5; -.
DR BioCyc; ARA:AT3G14130-MON; -.
DR BRENDA; 1.1.3.15; 399.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9LJH5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJH5; baseline and differential.
DR Genevisible; Q9LJH5; 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:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
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 Fatty acid metabolism; Flavoprotein; FMN; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..363
FT /note="Peroxisomal (S)-2-hydroxyacid oxidase GLO4"
FT /id="PRO_0000403407"
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 65
FT /note="M -> I (in Ref. 4; AAM61594)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> P (in Ref. 4; AAM61594)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> V (in Ref. 4; AAM61594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39878 MW; 19A62CDD8F9E1088 CRC64;
MDQIVNVDEF QELAKQALPK MYYDFYNGGA EDQHTLNENV QAFRRIMFRP RVLVDVSNID
MSTSMLGYPI SAPIMIAPTA MHKLAHPKGE IATAKAAAAC NTIMIVSFMS TCTIEEVASS
CNAVRFLQIY VYKRRDVTAQ IVKRAEKAGF KAIVLTVDVP RLGRREADIK NKMISPQLKN
FEGLVSTEVR PNEGSGVEAF ASSAFDASLS WKDIEWLRSI TKLPILVKGL LTREDALKAV
EAGVDGIVVS NHGARQLDYS PATITVLEEV VHAVKGRIPV LLDGGVRRGT DVFKALALGA
QAVLIGRPIV YGLAAKGEDG VKKVIDMLKN EFEITMALSG CPTIDDVTRN HVRTENERIK
SML
