ID A0A6A3Y3N8_9STRA Unreviewed; 387 AA.
AC A0A6A3Y3N8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase {ECO:0000313|EMBL:KAE9211485.1};
GN ORFNames=PF001_g16772 {ECO:0000313|EMBL:KAE9296647.1}, PF002_g18516
GN {ECO:0000313|EMBL:KAE9211485.1}, PF004_g16266
GN {ECO:0000313|EMBL:KAE9210149.1}, PF005_g17220
GN {ECO:0000313|EMBL:KAE9195612.1}, PF006_g16241
GN {ECO:0000313|EMBL:KAE9128604.1}, PF007_g17354
GN {ECO:0000313|EMBL:KAE9095510.1}, PF008_g16883
GN {ECO:0000313|EMBL:KAE9325412.1}, PF009_g18418
GN {ECO:0000313|EMBL:KAE8931520.1}, PF010_g16773
GN {ECO:0000313|EMBL:KAE9095259.1}, PF011_g16127
GN {ECO:0000313|EMBL:KAE8995908.1};
OS Phytophthora fragariae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporomycetes;
OC Peronosporales; Peronosporaceae; Phytophthora.
OX NCBI_TaxID=53985 {ECO:0000313|EMBL:KAE9211485.1, ECO:0000313|Proteomes:UP000440367};
RN [1] {ECO:0000313|Proteomes:UP000429523, ECO:0000313|Proteomes:UP000433483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:KAE9296647.1,
RC ECO:0000313|Proteomes:UP000437068}, BC-1
RC {ECO:0000313|EMBL:KAE9211485.1, ECO:0000313|Proteomes:UP000440367},
RC BC-23 {ECO:0000313|EMBL:KAE9210149.1,
RC ECO:0000313|Proteomes:UP000476176}, NOV-27
RC {ECO:0000313|EMBL:KAE9195612.1, ECO:0000313|Proteomes:UP000433483},
RC NOV-5 {ECO:0000313|EMBL:KAE9128604.1,
RC ECO:0000313|Proteomes:UP000440732}, NOV-71
RC {ECO:0000313|EMBL:KAE9095510.1, ECO:0000313|Proteomes:UP000441208},
RC NOV-77 {ECO:0000313|EMBL:KAE9325412.1,
RC ECO:0000313|Proteomes:UP000486351}, NOV-9
RC {ECO:0000313|EMBL:KAE8931520.1, ECO:0000313|Proteomes:UP000429523},
RC ONT-3 {ECO:0000313|EMBL:KAE9095259.1,
RC ECO:0000313|Proteomes:UP000488956}, and SCRP245
RC {ECO:0000313|EMBL:KAE8995908.1, ECO:0000313|Proteomes:UP000460718};
RA Adams T.M., Armitage A.D., Sobczyk M.K., Bates H.J., Dunwell J.M.,
RA Nellist C.F., Harrison R.J.;
RT "Genomic investigation of the strawberry pathogen Phytophthora fragariae
RT indicates pathogenicity is determined by transcriptional variation in three
RT key races.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAE9211485.1}.
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DR EMBL; QXGF01001230; KAE8931520.1; -; Genomic_DNA.
DR EMBL; QXFW01001135; KAE8995908.1; -; Genomic_DNA.
DR EMBL; QXFX01001168; KAE9095259.1; -; Genomic_DNA.
DR EMBL; QXFZ01001170; KAE9095510.1; -; Genomic_DNA.
DR EMBL; QXGA01001117; KAE9128604.1; -; Genomic_DNA.
DR EMBL; QXGB01001174; KAE9195612.1; -; Genomic_DNA.
DR EMBL; QXGC01001142; KAE9210149.1; -; Genomic_DNA.
DR EMBL; QXGD01001221; KAE9211485.1; -; Genomic_DNA.
DR EMBL; QXGE01001169; KAE9296647.1; -; Genomic_DNA.
DR EMBL; QXFY01001184; KAE9325412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A3Y3N8; -.
DR OrthoDB; 25826at2759; -.
DR Proteomes; UP000429523; Unassembled WGS sequence.
DR Proteomes; UP000433483; Unassembled WGS sequence.
DR Proteomes; UP000437068; Unassembled WGS sequence.
DR Proteomes; UP000440367; Unassembled WGS sequence.
DR Proteomes; UP000440732; Unassembled WGS sequence.
DR Proteomes; UP000441208; Unassembled WGS sequence.
DR Proteomes; UP000460718; Unassembled WGS sequence.
DR Proteomes; UP000476176; Unassembled WGS sequence.
DR Proteomes; UP000486351; Unassembled WGS sequence.
DR Proteomes; UP000488956; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR FunFam; 3.20.20.70:FF:000056; hydroxyacid oxidase 2; 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:SF149; 2-HYDROXYACID OXIDASE 2; 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|PIRSR:PIRSR000138-2};
KW FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000433483}.
FT DOMAIN 7..376
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 33
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 86..88
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 115
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 141
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 143
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 169
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 178
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 247
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 269
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 271
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 274
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 302..306
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 325..326
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 387 AA; 41657 MW; D6AF65961867B1AC CRC64;
MPKIVPGSDG TPLNVLEYEE YAREYLPKNA FDYYASGADD MVTLRENREA FKRLVLHPRV
LRDVSKMDTS TTLLGHRVSS PVCVAPSAMH RMAHPDGEIA STTATAKADA CYILSTISTT
SLEDVAAANS AANAHALRWY QLYVFKDREI TRGLVQRAEK AGYKAIVLTV DTPMLGHREP
DVRNRFSLPG HLTMANFAEV GGEHEHGVSS LQDSGLAHYV GELFDLTLNW NDVKWLKSIT
KLPVVVKGVL SPEDAKIAVD LGCEGVLVSN HGARQLDGVA ATIDALPAIV QAVGGRAEVY
LDGGVRRGTD VFKALALGAR AVFLGRPVLF GLAHSGEAGV SNVLRILNEE LRHAMLFSGT
ATLADIGPAY VRRGVPPLPS SLLPNAS
//
