GLO1_ORYSI
ID GLO1_ORYSI Reviewed; 369 AA.
AC B8AKX6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Glycolate oxidase 1;
DE Short=GOX 1;
DE Short=OsGLO1;
DE EC=1.1.3.15 {ECO:0000250|UniProtKB:Q10CE4};
DE AltName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO1;
DE AltName: Full=Short chain alpha-hydroxy acid oxidase GLO1;
GN Name=GLO1; ORFNames=OsI_13800;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
CC -!- FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a
CC reduction of O2 to H2O2 (By similarity). Is a key enzyme in
CC photorespiration in plants (By similarity). Can exert a strong
CC regulation over photosynthesis, possibly through a feed-back inhibition
CC on Rubisco activase. Does not seem to play a role in oxalate
CC accumulation (By similarity). {ECO:0000250|UniProtKB:A0A3L6E0R4,
CC ECO:0000250|UniProtKB:Q10CE4}.
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:0000250|UniProtKB:Q10CE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC Evidence={ECO:0000250|UniProtKB:Q10CE4};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05414};
CC -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2-
CC phosphoglycolate: step 2/3. {ECO:0000250|UniProtKB:A0A3L6E0R4}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with rice dwarf virus
CC (RDV) P8. This interaction promotes viral P8 relocation to virus
CC factories peripheral to peroxisomes (By similarity).
CC {ECO:0000250|UniProtKB:P05414, ECO:0000250|UniProtKB:Q10CE4}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q10CE4}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR EMBL; CM000128; EEC76290.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AKX6; -.
DR SMR; B8AKX6; -.
DR STRING; 39946.B8AKX6; -.
DR PRIDE; B8AKX6; -.
DR EnsemblPlants; BGIOSGA013686-TA; BGIOSGA013686-PA; BGIOSGA013686.
DR Gramene; BGIOSGA013686-TA; BGIOSGA013686-PA; BGIOSGA013686.
DR HOGENOM; CLU_020639_0_0_1; -.
DR OMA; WSYVAGG; -.
DR UniPathway; UPA00951; UER00912.
DR Proteomes; UP000007015; Chromosome 3.
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:0009854; P:oxidative photosynthetic carbon pathway; 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 3: Inferred from homology;
KW Flavoprotein; FMN; Glycolate pathway; Host-virus interaction;
KW Oxidoreductase; Peroxisome; Photorespiration; Reference proteome.
FT CHAIN 1..369
FT /note="Glycolate oxidase 1"
FT /id="PRO_0000403410"
FT DOMAIN 1..360
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT MOTIF 367..369
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 25
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
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="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT BINDING 156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P05414"
FT BINDING 165
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
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 255
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
FT BINDING 258
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000250|UniProtKB:Q9UJM8"
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 SITE 109
FT /note="Involved in determining the substrate specificity of
FT glycolate oxidase"
FT /evidence="ECO:0000250|UniProtKB:P05414"
SQ SEQUENCE 369 AA; 40384 MW; B14AF6A0E95883FF CRC64;
MGEITNVMEY QAIAKQKLPK MIYDYYASGA EDEWTLKENR EAFSRILFRP RILIDVSKID
MSATVLGFKI SMPIMIAPSA MQKMAHPDGE YATARAASAA GTIMTLSSWA TSSVEEVAST
GPGIRFFQLY VYKDRNVVEQ LVRRAERAGF KAIALTVDTP RLGRREADIK NRFVLPPYLT
LKNFEGLDLA EMDKSNDSGL ASYVAGQIDR TLSWKDVKWL QSITSLPILV KGVITAEDAR
LAVHSGAAGI IVSNHGARQL DYVPATISAL EEVVTAAAGR IPVYLDGGVR RGTDVFKALA
LGAAGVFIGR PVVFALAAEG EAGVRNVLRM MREEFELTMA LSGCTSLADI TRAHIYTDAD
RLARPFPRL
