ID A0A3B6C2K0_WHEAT Unreviewed; 373 AA.
AC A0A3B6C2K0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=(S)-2-hydroxy-acid oxidase {ECO:0000256|ARBA:ARBA00013087};
DE EC=1.1.3.15 {ECO:0000256|ARBA:ARBA00013087};
GN ORFNames=CFC21_022478 {ECO:0000313|EMBL:KAF7007545.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2B02G194600.1};
RN [1] {ECO:0000313|EMBL:KAF7007545.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7007545.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS2B02G194600.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS2B02G194600.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS2B02G194600.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7007545.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7007545.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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 EMBL; CM022215; KAF7007545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6C2K0; -.
DR EnsemblPlants; TraesCS2B02G194600.1; TraesCS2B02G194600.1; TraesCS2B02G194600.
DR Gramene; TraesCAD_scaffold_037388_01G000100.1; TraesCAD_scaffold_037388_01G000100.1; TraesCAD_scaffold_037388_01G000100.
DR Gramene; TraesCLE_scaffold_005433_01G000300.1; TraesCLE_scaffold_005433_01G000300.1; TraesCLE_scaffold_005433_01G000300.
DR Gramene; TraesCS2B02G194600.1; TraesCS2B02G194600.1; TraesCS2B02G194600.
DR Gramene; TraesCS2B03G0469600.2; TraesCS2B03G0469600.2.CDS; TraesCS2B03G0469600.
DR Gramene; TraesPAR_scaffold_011294_01G000300.1; TraesPAR_scaffold_011294_01G000300.1; TraesPAR_scaffold_011294_01G000300.
DR Gramene; TraesROB_scaffold_012773_01G000100.1; TraesROB_scaffold_012773_01G000100.1; TraesROB_scaffold_012773_01G000100.
DR Gramene; TraesWEE_scaffold_006737_01G000300.1; TraesWEE_scaffold_006737_01G000300.1; TraesWEE_scaffold_006737_01G000300.
DR OMA; IEMNMVF; -.
DR OrthoDB; 276514at2759; -.
DR Proteomes; UP000019116; Chromosome 2B.
DR Proteomes; UP000815260; Chromosome 2B.
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:0051707; P:response to other organism; IEA:UniProt.
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.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000138-2};
KW FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT DOMAIN 1..367
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 27
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 80..82
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 109
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
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 132
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 167
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 238
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 260
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 262
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 265
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 293..297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 316..317
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 373 AA; 40439 MW; 782F8F3307419DCF CRC64;
MENNLPVNIR EYQELAKKAL PKMHYDYING GAEDEHTLRD NIAAYGRILL RPRVLVDVSN
IDMSINLLGY DMPSPIIVAP TGSHKLANPE GEVATARAAA SCNTLMVLSF SASCKIEEVA
SSCNAIRFYQ LYVFKNRDVS ATLVRRAESH GFKAIVLTVD TPMLGRREAD IRNKMVAPAN
ANLEGLMPID DLDTARISHL QTGGSKLEKY ARDTLDPSLS WKDVEWLKSI TSLPILLKGI
VTAEDARKAV EAGAAGIIVS NHGARQLDYA PATISALEEV VKAVVGAVPV LVDGGVRRGT
DLLKALALGA RAVMVGRPVL YGLAARGQAG AKHVIEMLNR ELELAMALCG CRSVAEITRD
RVQTEGDRFR SLL
//
