ID   HAOX_ORYSJ              Reviewed;         366 AA.
AC   Q8H3I4; A0A0P0X8U9; B9FU85;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 2.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO4;
DE            EC=1.1.3.15 {ECO:0000250|UniProtKB:Q9LJH5};
DE   AltName: Full=Glycolate oxidase 4;
DE            Short=GOX 4;
DE            Short=OsGLO4;
DE   AltName: Full=Short chain alpha-hydroxy acid oxidase GLO4;
GN   Name=GLO4; OrderedLocusNames=Os07g0616500;
GN   ORFNames=B1056G08.112, OsJ_25131;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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   INTERACTION WITH CATB AND CATC.
RC   STRAIN=cv. Zhonghua 11;
RX   PubMed=26900141; DOI=10.1016/j.molp.2016.02.002;
RA   Zhang Z., Xu Y., Xie Z., Li X., He Z.-H., Peng X.-X.;
RT   "Association-dissociation of glycolate oxidase with catalase in rice: a
RT   potential switch to modulate intracellular H2O2 levels.";
RL   Mol. Plant 9:737-748(2016).
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. May be involved in a general medium- and long-chain fatty acid
CC       catabolic pathway such as alpha-oxidation.
CC       {ECO:0000250|UniProtKB:Q9LJH5}.
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:0000250|UniProtKB:Q9LJH5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790;
CC         Evidence={ECO:0000250|UniProtKB:Q9LJH5};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05414};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000250|UniProtKB:Q9LJH5}.
CC   -!- SUBUNIT: Homotetramer (By similarity). Binds to CATB and CATC; these
CC       interactions are disturbed by alpha-hydroxy-2-pyridinemethanesulfonic
CC       acid (HPMS) and salicylic acid (SA) (PubMed:26900141).
CC       {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEE67592.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AP004988; BAC79990.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF22190.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT02654.1; -; Genomic_DNA.
DR   EMBL; CM000144; EEE67592.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AK071738; BAG92663.1; -; mRNA.
DR   RefSeq; XP_015647067.1; XM_015791581.1.
DR   RefSeq; XP_015647068.1; XM_015791582.1.
DR   RefSeq; XP_015647069.1; XM_015791583.1.
DR   RefSeq; XP_015647070.1; XM_015791584.1.
DR   AlphaFoldDB; Q8H3I4; -.
DR   SMR; Q8H3I4; -.
DR   STRING; 39947.Q8H3I4; -.
DR   PaxDb; 39947-Q8H3I4; -.
DR   EnsemblPlants; Os07t0616500-01; Os07t0616500-01; Os07g0616500.
DR   GeneID; 4343908; -.
DR   Gramene; Os07t0616500-01; Os07t0616500-01; Os07g0616500.
DR   KEGG; osa:4343908; -.
DR   eggNOG; KOG0538; Eukaryota.
DR   HOGENOM; CLU_020639_0_0_1; -.
DR   InParanoid; Q8H3I4; -.
DR   OMA; WADFQYE; -.
DR   OrthoDB; 276514at2759; -.
DR   PlantReactome; R-OSA-1119312; Photorespiration.
DR   PlantReactome; R-OSA-1119596; Glutamate biosynthesis I.
DR   UniPathway; UPA00199; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; ISS:UniProtKB.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0098586; P:cellular response to virus; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009853; P:photorespiration; ISS:UniProtKB.
DR   GO; GO:0010109; P:regulation of photosynthesis; ISS:UniProtKB.
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:SF67; PEROXISOMAL (S)-2-HYDROXYACID OXIDASE GLO3-RELATED; 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   SMART; SM01240; IMPDH; 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; Q8H3I4; OS.
PE   1: Evidence at protein level;
KW   Fatty acid metabolism; Flavoprotein; FMN; Lipid metabolism; Oxidoreductase;
KW   Peroxisome; Reference proteome.
FT   CHAIN           1..366
FT                   /note="Peroxisomal (S)-2-hydroxy-acid oxidase GLO4"
FT                   /id="PRO_0000403415"
FT   DOMAIN          1..360
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   MOTIF           364..366
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        255
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         27
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         80..82
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         109
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         130..132
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         132
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         158
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         167
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         231
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         253
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         258
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         286..290
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   BINDING         309..310
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P05414"
FT   CONFLICT        313
FT                   /note="F -> L (in Ref. 4; EEE67592)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="E -> D (in Ref. 4; EEE67592)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  39764 MW;  73FCBAD72CC9B9F5 CRC64;
     MEDNLPVNVR EYQELAKKAL PKMAYDYING GAEDEHTLRE NIAAYTRIIL RPRVLVDVSK
     IDMSTTLLGY TMRSPIIVAP TGGHKLAHPE GEKATARAAA SCNAIMVLSF SSSCKIEDVA
     SSCNAIRFYQ LYVYKNRNVS ATLVRRAESC GFKALLLTVD TPMLGRREAD IRNKMVFPRS
     GNLEGLMTTD DHDTTNGSQL ERFARATLDP SLSWKDIEWL KSITSMPIFL KGIVTAEDAR
     RAVEAGVAGV IVSNHGARQL DYAPATIAAL EEVVRAVAGA VPVLVDGGIR RGTDVFKALA
     LGARAVMVGR PVFFGLAARG EAGARHVIEM LNGELEVAMA LCGCRSVGEI TRSHVMTEGD
     RIRSLL
//