GOX1_MAIZE
ID GOX1_MAIZE Reviewed; 369 AA.
AC A0A3L6E0R4; C0P702;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Glycolate oxidase 1 {ECO:0000303|PubMed:18805949, ECO:0000303|PubMed:25416784};
DE Short=GOX {ECO:0000303|PubMed:25416784};
DE EC=1.1.3.15 {ECO:0000269|PubMed:25416784};
GN Name=GO1 {ECO:0000303|PubMed:18805949, ECO:0000303|PubMed:25416784};
GN ORFNames=Zm00014a_001774 {ECO:0000312|EMBL:PWZ13502.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Missouri 17; TISSUE=Seedling;
RX PubMed=30061735; DOI=10.1038/s41588-018-0182-0;
RA Sun S., Zhou Y., Chen J., Shi J., Zhao H., Zhao H., Song W., Zhang M.,
RA Cui Y., Dong X., Liu H., Ma X., Jiao Y., Wang B., Wei X., Stein J.C.,
RA Glaubitz J.C., Lu F., Yu G., Liang C., Fengler K., Li B., Rafalski A.,
RA Schnable P.S., Ware D.H., Buckler E.S., Lai J.;
RT "Extensive intraspecific gene order and gene structural variations between
RT Mo17 and other maize genomes.";
RL Nat. Genet. 50:1289-1295(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=18805949; DOI=10.1104/pp.108.128439;
RA Zelitch I., Schultes N.P., Peterson R.B., Brown P., Brutnell T.P.;
RT "High glycolate oxidase activity is required for survival of maize in
RT normal air.";
RL Plant Physiol. 149:195-204(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION
RP MECHANISM, AND ACTIVE SITE.
RX PubMed=25416784; DOI=10.1074/jbc.m114.618629;
RA Dellero Y., Mauve C., Boex-Fontvieille E., Flesch V., Jossier M.,
RA Tcherkez G., Hodges M.;
RT "Experimental evidence for a hydride transfer mechanism in plant glycolate
RT oxidase catalysis.";
RL J. Biol. Chem. 290:1689-1698(2015).
CC -!- FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a
CC reduction of O2 to H2O2 (PubMed:25416784). Is an essential enzyme in
CC photorespiration in plants (PubMed:18805949). Photorespiration plays a
CC vital role in C4 photosynthesis in Z.mays and is essential for maize
CC seedling development and maintaining low (non-toxic) levels of
CC glycolate (PubMed:18805949). {ECO:0000269|PubMed:18805949,
CC ECO:0000269|PubMed:25416784}.
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:0000269|PubMed:25416784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC Evidence={ECO:0000305|PubMed:25416784};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05414};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:P05414};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for glycolate (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:25416784};
CC Note=kcat is 34.13 sec(-1) (at pH 8 and 30 degrees Celsius).
CC {ECO:0000269|PubMed:25416784};
CC -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2-
CC phosphoglycolate: step 2/3. {ECO:0000269|PubMed:18805949}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P05414}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305|PubMed:18805949}.
CC -!- DISRUPTION PHENOTYPE: The mutant shows deficiency in glycolate oxidase
CC activity and is non-viable in air; leaves become necrotic within 7 days
CC and plants die within 15 days. When the mutant cells are shifted from
CC high CO2 to air in light, they accumulate glycolate linearly for 6
CC hours to levels 7-fold higher than wild type and 11-fold higher after
CC 25 hours. {ECO:0000269|PubMed:18805949}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; NCVQ01000008; PWZ13502.1; -; Genomic_DNA.
DR EMBL; BT064071; ACN28768.1; -; mRNA.
DR RefSeq; NP_001146005.1; NM_001152533.1.
DR RefSeq; XP_008651329.1; XM_008653107.1.
DR EnsemblPlants; Zm00001eb300130_T002; Zm00001eb300130_P002; Zm00001eb300130.
DR GeneID; 100279535; -.
DR Gramene; Zm00001eb300130_T002; Zm00001eb300130_P002; Zm00001eb300130.
DR KEGG; zma:100279535; -.
DR HOGENOM; CLU_020639_0_0_1; -.
DR OrthoDB; 879633at2759; -.
DR UniPathway; UPA00951; UER00912.
DR Proteomes; UP000007305; Chromosome 7.
DR Proteomes; UP000251960; Chromosome 7.
DR ExpressionAtlas; A0A3L6E0R4; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:0009854; P:oxidative photosynthetic carbon pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
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; Glycolate pathway; Oxidoreductase; Peroxisome;
KW Photorespiration; Reference proteome.
FT CHAIN 1..369
FT /note="Glycolate oxidase 1"
FT /id="PRO_0000454911"
FT DOMAIN 1..360
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:25416784"
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"
FT CONFLICT 91
FT /note="Y -> N (in Ref. 2; ACN28768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 40095 MW; 0D608B3368DCCF8C CRC64;
MGEITNVMEY QAIAKQKLPK MAYDYYASGA EDEWTLQENR EAFSRILFRP RILIDVSKID
MTTTVLGFKI SMPIMVAPTA MQKMAHPDGE YATARAAAAA GTIMTLSSWA TSSVEEVAST
GPGIRFFQLY VYKDRKVVEQ LVRRAERAGF KAIALTVDTP RLGRREADIK NRFVLPPHLT
LKNFEGLDLG KMDQAADSGL ASYVAGQVDR TLSWKDVKWL QTITTLPILV KGVLTAEDTR
LAVANGAAGI IVSNHGARQL DYVPATISAL EEVVKAARGQ LPVFVDGGVR RGTDVFKALA
LGAAGVFVGR PVVFSLAAAG EAGVSNVLRM LRDEFELTMA LSGCTSLAEI TRKHIITESD
KLSAIPSRL
