HAOX_ORYSJ
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 03-AUG-2022, entry version 120.
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; 4530.OS07T0616500-01; -.
DR PaxDb; Q8H3I4; -.
DR PRIDE; 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; FQYEIYL; -.
DR OrthoDB; 879633at2759; -.
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 Genevisible; Q8H3I4; OS.
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; -; 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..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
