ID A0A453D070_AEGTS Unreviewed; 341 AA.
AC A0A453D070;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-OCT-2025, entry version 27.
DE RecName: Full=(S)-2-hydroxy-acid oxidase {ECO:0000256|ARBA:ARBA00013087};
DE EC=1.1.3.15 {ECO:0000256|ARBA:ARBA00013087};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv21032700.1, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv21032700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|EnsemblPlants:AET2Gv21032700.1};
RX PubMed=29143815;
RA Luo M.C., Gu Y.Q., Puiu D., Wang H., Twardziok S.O., Deal K.R., Huo N.,
RA Zhu T., Wang L., Wang Y., McGuire P.E., Liu S., Long H., Ramasamy R.K.,
RA Rodriguez J.C., Van S.L., Yuan L., Wang Z., Xia Z., Xiao L., Anderson O.D.,
RA Ouyang S., Liang Y., Zimin A.V., Pertea G., Qi P., Bennetzen J.L., Dai X.,
RA Dawson M.W., Muller H.G., Kugler K., Rivarola-Duarte L., Spannagl M.,
RA Mayer K.F.X., Lu F.H., Bevan M.W., Leroy P., Li P., You F.M., Sun Q.,
RA Liu Z., Lyons E., Wicker T., Salzberg S.L., Devos K.M., Dvorak J.;
RT "Genome sequence of the progenitor of the wheat D genome Aegilops
RT tauschii.";
RL Nature 551:498-502(2017).
RN [4] {ECO:0000313|EnsemblPlants:AET2Gv21032700.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
RN [5] {ECO:0000313|EnsemblPlants:AET2Gv21032700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|EnsemblPlants:AET2Gv21032700.1};
RX PubMed=34515796;
RA Wang L., Zhu T., Rodriguez J.C., Deal K.R., Dubcovsky J., McGuire P.E.,
RA Lux T., Spannagl M., Mayer K.F.X., Baldrich P., Meyers B.C., Huo N.,
RA Gu Y.Q., Zhou H., Devos K.M., Bennetzen J.L., Unver T., Budak H.,
RA Gulick P.J., Galiba G., Kalapos B., Nelson D.R., Li P., You F.M., Luo M.C.,
RA Dvorak J.;
RT "Aegilops tauschii genome assembly Aet v5.0 features greater sequence
RT contiguity and improved annotation.";
RL G3 (Bethesda) 0:0-0(2021).
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:0000256|ARBA:ARBA00036241};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC Evidence={ECO:0000256|ARBA:ARBA00036241};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2-
CC phosphoglycolate: step 2/3. {ECO:0000256|ARBA:ARBA00004923}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
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DR AlphaFoldDB; A0A453D070; -.
DR EnsemblPlants; AET2Gv21032700.1; AET2Gv21032700.1; AET2Gv21032700.
DR Gramene; AET2Gv21032700.1; AET2Gv21032700.1; AET2Gv21032700.
DR Proteomes; UP000015105; Chromosome 2D.
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-KW.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR FunFam; 3.20.20.70:FF:000063; peroxisomal (S)-2-hydroxy-acid oxidase GLO1; 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:SF70; GLYCOLATE OXIDASE 3; 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 SUPFAM; SSF51395; FMN-linked oxidoreductases; 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 {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR000138-
KW 2}; FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000138-2};
KW Glycolate pathway {ECO:0000256|ARBA:ARBA00022594};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105}.
FT DOMAIN 1..334
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 52..54
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 81
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 102
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 104
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 139
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 205
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 227
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 229
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 232
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 260..264
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 283..284
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 341 AA; 37334 MW; 854B38FEC76BF87E CRC64;
ASGAEDQWTL NENREAFSRI LFRPRVLIDV SHINMATNIL GFDVSMPIMI APTAMQKMAH
PEGELATARA AASAGTIMTL SSWATSSVER VNSVGPGIRF FQLYVYKDRN IVRQLVKRAE
MAGFKAIALT VDTPRLGRRE ADIKNRFNLP PHLVLENFAA LDLGKMDKTD DSGLASYVAS
QVDQSLCWED VRWLQTITSL PILVKGVMTA EDTRIAIEYG AAGIIVSNHG ARQLDYVPAT
ISCLEEVVRE AKGRLPVFLD GGVRRGTDVF KALALGAAGV FIGRPVLYSL AVDGEAGVRK
VLQMLRDELE LAMALSGCPS LRDITRAHVV TDGDRIRRAR L
//
